1P5H
Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes
Summary for 1P5H
| Entry DOI | 10.2210/pdb1p5h/pdb |
| Related | 1P5R |
| Descriptor | Formyl-coenzyme A transferase (2 entities in total) |
| Functional Keywords | coa-transferase, oxalate, oxalate degradation, intertwined, knotted fold, caib-baif family, transferase |
| Biological source | Oxalobacter formigenes |
| Cellular location | Cytoplasm: O06644 |
| Total number of polymer chains | 2 |
| Total formula weight | 94761.79 |
| Authors | Ricagno, S.,Jonsson, S.,Richards, N.,Lindqvist, Y. (deposition date: 2003-04-27, release date: 2003-07-29, Last modification date: 2024-02-14) |
| Primary citation | Ricagno, S.,Jonsson, S.,Richards, N.,Lindqvist, Y. Formyl-CoA Transferase encloses the CoA binding site at the interface of an interlocked dimer Embo J., 22:3210-3219, 2003 Cited by PubMed Abstract: 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. PubMed: 12839984DOI: 10.1093/emboj/cdg333 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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