1p5h: Difference between revisions

Revision as of 20:57, 28 July 2008

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File:1p5h.png

Template:STRUCTURE 1p5h

Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenesCrystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes

Template:ABSTRACT PUBMED 12839984

About this StructureAbout this Structure

1P5H is a Single protein structure of sequence from Oxalobacter formigenes. Full crystallographic information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12839984}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Oxalate]]
 [[Category: Oxalate degradation]]
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