SCP2-thiolase: Difference between revisions
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==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> == | ==Structure of the zebrafish SCP2-thiolase <ref>PMID:30573650</ref> == | ||
<StructureSection load='6hsp' size='350' side='right' caption=' | <StructureSection load='6hsp' size='350' side='right' caption='Zebrafish SCP2-thiolase complex with CoA and octanoyl-CoA (PDB code [[6hsp]]) ' scene=''> | ||
==Introduction== | ==Introduction== | ||
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 '''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 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>. | 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. | 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/2'>dimer interface</scene>. | ||
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). | 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). | ||
== Function and Disease== | == Function and Disease== | ||
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== Structural highlights == | == 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/10'>morph</scene>. | ||
