SCP2-thiolase: Difference between revisions

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==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==

==Introduction==

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.

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.

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>.

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.

The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.

~~The active site is at the~~ <scene name='80/809821/6hsp-~~dimer_active_site~~/1'>~~dimer interface~~</scene>

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).

The ~~active site is shaped by~~ the ~~residues of~~ <~~scene name='80~~/~~809821/6hsp~~-~~dimer~~-~~catalytic~~-~~residues/2'>four loops</scene>~~

== Function and Disease==

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>

~~== Function ==~~

~~Here '''something''' about ''function''~~ <ref>pmid 16685654</ref>

~~== Disease ==~~

~~== Relevance ==~~

== Structural highlights ==

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>.

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>.

SCP2-thiolase: Difference between revisions

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 ==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> ==
-<StructureSection load='6hsp' size='350' side='right' caption='This is the asymmetric unit. Resolution 1.7Å. ' scene=''>
+<StructureSection load='6hsp' size='350' side='right' caption='Zebrafish SCP2-thiolase complex with CoA and octanoyl-CoA (PDB code [[6hsp]]) ' scene=''>
+==Introduction==
+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.
-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.
 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>.
+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.
+The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>.
-The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene>
+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).
-The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene>
+== Function and Disease==
+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>
-== Function ==
-Here '''something''' about ''function'' <ref>pmid 16685654</ref>
-== Disease ==
-== Relevance ==
 == Structural highlights ==
+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>.
-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>.