1p5r
From Proteopedia
(New page: 200px<br /><applet load="1p5r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p5r, resolution 2.50Å" /> '''Formyl-CoA Transfera...) |
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| - | [[Image:1p5r.jpg|left|200px]]<br /><applet load="1p5r" size=" | + | [[Image:1p5r.jpg|left|200px]]<br /><applet load="1p5r" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1p5r, resolution 2.50Å" /> | caption="1p5r, resolution 2.50Å" /> | ||
'''Formyl-CoA Transferase in complex with Coenzyme A'''<br /> | '''Formyl-CoA Transferase in complex with Coenzyme A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Formyl-CoA transferase catalyses transfer of CoA from formate to oxalate | + | 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== | ==About this Structure== | ||
| - | 1P5R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes] with COA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1P5R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes] with <scene name='pdbligand=COA:'>COA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5R OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxalate degradation]] | [[Category: oxalate degradation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:28 2008'' |
Revision as of 12:25, 21 February 2008
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Formyl-CoA Transferase in complex with Coenzyme A
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
1P5R is a Single protein structure of sequence from Oxalobacter formigenes with as ligand. 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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