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https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Rik+Wierenga Proteopedia - User contributions [en] 2026-10-01T01:14:32Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Scp2thiolase&diff=3026430 Scp2thiolase 2019-04-13T19:52:45Z

<p>Rik Wierenga: Scp2thiolase moved to SCP2-thiolase: now the name is correct</p> <hr /> <div>#REDIRECT [[SCP2-thiolase]]</div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026429 SCP2-thiolase 2019-04-13T19:52:45Z

<p>Rik Wierenga: Scp2thiolase moved to SCP2-thiolase: now the name is correct</p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> ==Introduction==<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref name="fingerprint">PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> Each subunit can be divided in a <scene name='80/809821/6hsp-dimer-domain-coloring/1'>color coded</scene> N-terminal domain, a loop domain and a C-terminal domain.<br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> Four loops provide critically important catalytic residues. These loops have characteristic sequence fingerprints <ref name="fingerprint"/>. These <scene name='80/809821/6hsp-dimer-catalytic-residues/3'>four loops</scene> are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> == Structural highlights == <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026423 SCP2-thiolase 2019-04-13T13:16:21Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> ==Introduction==<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref name="fingerprint">PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> Each subunit can be divided in a <scene name='80/809821/6hsp-dimer-domain-coloring/1'>color coded</scene> N-terminal domain, a loop domain and a C-terminal domain.<br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> Four loops provide critically important catalytic residues. These loops have characteristic sequence fingerprints <ref name="fingerprint"/>. These <scene name='80/809821/6hsp-dimer-catalytic-residues/3'>four loops</scene> are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> == Structural highlights == <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026422 SCP2-thiolase 2019-04-13T13:14:14Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> ==Introduction==<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref name="fingerprint">PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> <br /> <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> Each subunit can be divided in a <scene name='80/809821/6hsp-dimer-domain-coloring/1'>color coded</scene> N-terminal domain, a loop domain and a C-terminal domain.<br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> Four loops provide critically important catalytic residues. These loops have characteristic sequence fingerprints. These <scene name='80/809821/6hsp-dimer-catalytic-residues/3'>four loops</scene> are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> == Structural highlights == <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026421 SCP2-thiolase 2019-04-13T13:11:05Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> ==Introduction==<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> Each subunit can be divided in a <scene name='80/809821/6hsp-dimer-domain-coloring/1'>color coded</scene> N-terminal domain, a loop domain and a C-terminal domain.<br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> Four loops provide critically important catalytic residues. These loops have characteristic sequence fingerprints. These <scene name='80/809821/6hsp-dimer-catalytic-residues/3'>four loops</scene> are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> == Structural highlights == <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026420 SCP2-thiolase 2019-04-13T13:10:14Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> ==Introduction==<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> Each subunit can be divided in a <scene name='80/809821/6hsp-dimer-domain-coloring/1'>color coded</scene> N-terminal domain, a loop domain and a C-terminal domain.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> Four loops provide critically important catalytic residues. These loops have characteristic sequence fingerprints. These <scene name='80/809821/6hsp-dimer-catalytic-residues/3'>four loops</scene> are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> == Structural highlights == <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026419 SCP2-thiolase 2019-04-13T13:09:28Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> ==Introduction==<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> Each subunit can be divided in a <scene name='80/809821/6hsp-dimer-domain-coloring/1'>color coded</scene> N-terminal domain, a loop domain and a C-terminal domain.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> Four loops provide critically important catalytic residues. These loops have characteristic sequence fingerprints. These <scene name='80/809821/6hsp-dimer-catalytic-residues/3'>four loops</scene> are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026418 SCP2-thiolase 2019-04-13T13:09:02Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> ==Introduction==<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> Each subunit can be divided in a <scene name='80/809821/6hsp-dimer-domain-coloring/1'>color coded</scene> N-terminal domain, a loop domain and a C-terminal domain.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> Four loops provide critically important catalytic residues. These loops have characteristic sequence fingerprints. These <scene name='80/809821/6hsp-dimer-catalytic-residues/3'>four loops</scene> are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026417 SCP2-thiolase 2019-04-13T13:08:42Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> ==Introduction==<br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> Each subunit can be divided in a <scene name='80/809821/6hsp-dimer-domain-coloring/1'>color coded</scene> N-terminal domain, a loop domain and a C-terminal domain.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> Four loops provide critically important catalytic residues. These loops have characteristic sequence fingerprints. These <scene name='80/809821/6hsp-dimer-catalytic-residues/3'>four loops</scene> are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026416 SCP2-thiolase 2019-04-13T13:08:05Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> ==Introduction==<br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> Each subunit can be divided in a <scene name='80/809821/6hsp-dimer-domain-coloring/1'>color coded</scene> N-terminal domain, a loop domain and a C-terminal domain.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> Four loops provide critically important catalytic residues. These loops have characteristic sequence fingerprints. These <scene name='80/809821/6hsp-dimer-catalytic-residues/3'>four loops</scene> are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> <br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026250 SCP2-thiolase 2019-04-11T15:12:46Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> ==Introduction==<br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> Each subunit can be divided in a <scene name='80/809821/6hsp-dimer-domain-coloring/1'>color coded</scene> N-terminal domain, a loop domain and a C-terminal domain.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> These <scene name='80/809821/6hsp-dimer-catalytic-residues/3'>four loops</scene> are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> <br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026249 SCP2-thiolase 2019-04-11T15:11:14Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> ==Introduction==<br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> Each subunit can be divided in a <scene name='80/809821/6hsp-dimer-domain-coloring/1'>color coded</scene> N-terminal domain, a loop domain and a C-terminal domain.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene>.<br /> <br /> These <scene name='80/809821/6hsp-dimer-catalytic-residues/3'>four loops</scene> are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> <br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026248 SCP2-thiolase 2019-04-11T14:51:17Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> ==Introduction==<br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> Each subunit can be divided in a <scene name='80/809821/6hsp-dimer-domain-coloring/1'>color coded</scene> N-terminal domain, a loop domain and a C-terminal domain.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene>.<br /> <br /> These four loops are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> <br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026178 SCP2-thiolase 2019-04-10T18:53:18Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> ==Introduction==<br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> Each subunit can be divied in an N-termial domain, a loop domain and a C-terminal domain.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene>.<br /> <br /> These four loops are residues 87-89 (Nβ3-Nα3), 298-301 (Cβ2-Cα2), 347-349 (Cβ3-Cα3), 385-387 (Cβ4-Cβ5).<br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> <br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3026177 SCP2-thiolase 2019-04-10T18:47:17Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> ==Introduction==<br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> Each subunit can be divied in an N-termial domain, a loop domain and a C-terminal domain.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.<br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> <br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022995 SCP2-thiolase 2019-04-08T14:48:29Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> ==Introduction==<br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> <br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022991 SCP2-thiolase 2019-04-08T14:40:29Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> ==Introduction==<br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function and Disease==<br /> The SCP2 thiolase functions in the bile acid synthesis pathway <ref>pmid 9325339</ref>. SCP2-thiolase is synthesised as a larger protein, having the thiolase part and at the C-terminal end there is an extra domainn, the SCP2-domain. This domain has the sequence SKL at its C-terminus, which functions as the peroxisomal targetting sequence. In the peroxisome the SCP2-domain is proteolytically cleaved off, and the SCP2-thiolase chain is found to be present in the peroxisome, as described by Wanders and coworkers, who also described the deficiency symptoms in case the SCP2-thiolase is not properly expressed. <ref>pmid 16685654</ref><br /> <br /> <br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022988 SCP2-thiolase 2019-04-08T14:30:33Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> ==Introduction==<br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 16685654</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022985 SCP2-thiolase 2019-04-08T14:21:00Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 16685654</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/10'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022982 SCP2-thiolase 2019-04-08T14:08:29Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 16685654</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/9'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022979 SCP2-thiolase 2019-04-08T13:57:07Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 16685654</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/8'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022978 SCP2-thiolase 2019-04-08T13:52:20Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/7'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022977 SCP2-thiolase 2019-04-08T13:50:48Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/6'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022973 SCP2-thiolase 2019-04-08T13:30:32Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/5'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022972 SCP2-thiolase 2019-04-08T13:25:31Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/4'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022971 SCP2-thiolase 2019-04-08T13:19:38Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/3'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022970 SCP2-thiolase 2019-04-08T13:17:39Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' This is the asymmetric unit Resolution|1.7Å ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/3'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022969 SCP2-thiolase 2019-04-08T13:14:29Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' [[This is the asymmetric unit]] [[Resolution|1.7Å]] ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/3'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022968 SCP2-thiolase 2019-04-08T13:11:43Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' [[This is the asymmetric unit]] [[Resolution|1.7Å]] ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/Morph/2'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022967 SCP2-thiolase 2019-04-08T13:02:40Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' [[This is the asymmetric unit]] [[Resolution|1.7Å]] ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/morph/1'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022966 SCP2-thiolase 2019-04-08T13:01:32Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' [[This is the asymmetric unit]] [[Resolution|1.7Å]] ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/morph-movie/1'>morph</scene>.<br /> <br /> <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022965 SCP2-thiolase 2019-04-08T12:58:57Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' [[This is the asymmetric unit]] [[Resolution|1.7Å]] ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> When the A and B monomers are compared the structural differences can best be seen in this <scene name='80/809821/morph-movie/1'>morph</scene>.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022954 SCP2-thiolase 2019-04-08T09:09:45Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' [[This is the asymmetric unit]] [[Resolution|1.7Å]] ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022949 SCP2-thiolase 2019-04-08T08:50:25Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' [[This is the asymmetric unit]] [[Resolution|1.7Å]] ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/1'>four loops</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022944 SCP2-thiolase 2019-04-08T08:00:45Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' [[This is the asymmetric unit]] [[Resolution|1.7Å]] ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022943 SCP2-thiolase 2019-04-08T07:45:43Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' [[This is the asymmetric unit]] [[Resolution|1.7Å]] ' scene=''><br /> <br /> <br /> <br /> <br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022942 SCP2-thiolase 2019-04-08T07:44:33Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' [[This is the asymmetric unit]] [[Resolution|1.7Å]] ' scene=''><br /> <br /> caption='[[2jez]], [[Resolution|resolution]] 2.60&Aring;'<br /> <br /> 2.60&Aring<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022941 SCP2-thiolase 2019-04-08T07:41:09Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' [[This is the asymmetric unit]] [[Resolution|1.7Å]] ' scene=''><br /> <br /> caption='[[2jez]], [[Resolution|resolution]] 2.60&Aring;'<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022940 SCP2-thiolase 2019-04-08T07:38:45Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' [[This is the asymmetric unit]] ' scene=''><br /> <br /> caption='[[2jez]], [[Resolution|resolution]] 2.60&Aring;'<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022939 SCP2-thiolase 2019-04-08T07:37:55Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=' '''This is the asymmetric unit''' ' scene=''><br /> <br /> caption='[[2jez]], [[Resolution|resolution]] 2.60&Aring;'<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022938 SCP2-thiolase 2019-04-08T07:37:24Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption=''''This is the asymmetric unit'''' scene=''><br /> <br /> caption='[[2jez]], [[Resolution|resolution]] 2.60&Aring;'<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022937 SCP2-thiolase 2019-04-08T07:36:03Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='[[This is the asymmetric unit]]' scene=''><br /> <br /> caption='[[2jez]], [[Resolution|resolution]] 2.60&Aring;'<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022936 SCP2-thiolase 2019-04-08T07:34:40Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='this is the asymmetric unit' scene=''><br /> <br /> caption='[[2jez]], [[Resolution|resolution]] 2.60&Aring;'<br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022935 SCP2-thiolase 2019-04-08T07:25:51Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='' scene=''><br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes<ref>PMID:24825023</ref>. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022934 SCP2-thiolase 2019-04-08T07:23:36Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='' scene=''><br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>.<br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022933 SCP2-thiolase 2019-04-08T07:21:51Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='' scene=''><br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene><br /> <br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022932 SCP2-thiolase 2019-04-08T07:20:39Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='' scene=''><br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> <br /> <br /> The B-subunit is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene><br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022931 SCP2-thiolase 2019-04-08T07:16:52Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='' scene=''><br /> <br /> The SCP2-thiolase is a member of the thiolase family of enzymes. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. <br /> <br /> <br /> <br /> The B-subunit <scene name='80/809821/6hsp-dimer/5'>B-dimer</scene> is forming a dimer with its two-fold crystallographically related symmetry copy<br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022930 SCP2-thiolase 2019-04-08T07:06:48Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='' scene=''><br /> <br /> <br /> <br /> This is a default text for your page '''SandboxNewPage'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:30573650</ref> to the rescue.<br /> The B-subunit <scene name='80/809821/6hsp-dimer/5'>B-dimer</scene> is forming a dimer with its two-fold crystallographically related symmetry copy<br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga https://proteopedia.org/index.php?title=SCP2-thiolase&diff=3022929 SCP2-thiolase 2019-04-08T07:05:58Z

<p>Rik Wierenga: </p> <hr /> <div>==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==<br /> <StructureSection load='6hsp' size='350' side='right' caption='' scene=''><br /> <br /> This is a default text for your page '''SandboxNewPage'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:30573650</ref> to the rescue.<br /> The B-subunit <scene name='80/809821/6hsp-dimer/5'>B-dimer</scene> is forming a dimer with its two-fold crystallographically related symmetry copy<br /> == Function ==<br /> Here '''something''' about ''function'' <ref>pmid 25203508</ref><br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights == <br /> <br /> <scene name='80/809821/Morph/1'>morph</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Rik Wierenga