1p5h
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(New page: 200px<br /><applet load="1p5h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p5h, resolution 2.20Å" /> '''Crystal structure of...)
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Revision as of 21:22, 20 November 2007
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Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes
Overview
Formyl-CoA transferase catalyses transfer of CoA from formate to oxalate, in the first step of oxalate degradation by Oxalobacter formigenes, a, bacterium present in the intestinal flora which is implicated in oxalate, catabolism in mammals. Formyl-CoA transferase is a member of a family of, CoA-transferases for which no structural information is available. We now, report the three-dimensional structure of O.formigenes formyl-CoA, transferase, which reveals a novel fold and a very striking assembly of, the homodimer. The subunit is composed of a large and a small domain where, residues from both the N- and C-termini of the subunit are part of the, large domain. The linkers between the domains give the subunit a circular, shape with a hole in the middle. The enzyme monomers are tightly, interacting and are interlocked. This fold requires drastic rearrangement, of approximately 75 residues at the C-terminus for formation of the dimer., The structure of a complex of formyl-CoA transferase with CoA is also, reported and sets the scene for a mechanistic understanding of enzymes of, this family of CoA-transferases.
About this Structure
1P5H is a Single protein structure of sequence from Oxalobacter formigenes. Full crystallographic information is available from OCA.
Reference
Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer., Ricagno S, Jonsson S, Richards N, Lindqvist Y, EMBO J. 2003 Jul 1;22(13):3210-9. PMID:12839984
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