1p5h
From Proteopedia
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| - | [[Image:1p5h.jpg|left|200px]] | + | [[Image:1p5h.jpg|left|200px]] |
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| - | '''Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes''' | + | {{Structure |
| + | |PDB= 1p5h |SIZE=350|CAPTION= <scene name='initialview01'>1p5h</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= FRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=847 Oxalobacter formigenes]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1P5H is a [ | + | 1P5H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5H OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12839984 12839984] |
[[Category: Oxalobacter formigenes]] | [[Category: Oxalobacter formigenes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxalate degradation]] | [[Category: oxalate degradation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:20:10 2008'' |
Revision as of 11:20, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Gene: | FRC (Oxalobacter formigenes) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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