1p5h

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[[Image:1p5h.jpg|left|200px]]
[[Image:1p5h.jpg|left|200px]]
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{{Structure
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|PDB= 1p5h |SIZE=350|CAPTION= <scene name='initialview01'>1p5h</scene>, resolution 2.20&Aring;
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The line below this paragraph, containing "STRUCTURE_1p5h", creates the "Structure Box" on the page.
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|GENE= FRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=847 Oxalobacter formigenes])
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{{STRUCTURE_1p5h| PDB=1p5h | SCENE= }}
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|RELATEDENTRY=[[1p5r|1P5R]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5h OCA], [http://www.ebi.ac.uk/pdbsum/1p5h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p5h RCSB]</span>
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'''Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes'''
'''Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes'''
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[[Category: Ricagno, S.]]
[[Category: Ricagno, S.]]
[[Category: Richards, N.]]
[[Category: Richards, N.]]
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[[Category: caib-baif family]]
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[[Category: Caib-baif family]]
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[[Category: coa-transferase]]
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[[Category: Coa-transferase]]
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[[Category: intertwined]]
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[[Category: Intertwined]]
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[[Category: knotted fold]]
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[[Category: Knotted fold]]
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[[Category: oxalate]]
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[[Category: Oxalate]]
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[[Category: oxalate degradation]]
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[[Category: Oxalate degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:42:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:55:08 2008''
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Revision as of 01:42, 3 May 2008

Template:STRUCTURE 1p5h

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 Page seeded by OCA on Sat May 3 04:42:41 2008

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