1P5R

Formyl-CoA Transferase in complex with Coenzyme A

Summary for 1P5R

• Entry DOI: 10.2210/pdb1p5r/pdb
• Related: 1p5h
• Descriptor: Formyl-coenzyme A transferase, COENZYME A (3 entities in total)
• Functional Keywords: coa-transferase, oxalate, oxalate degradation, intertwined, knotted fold, caib-baif family, coa complex, transferase
• Biological source: Oxalobacter formigenes
• Cellular location: Cytoplasm: O06644
• Total number of polymer chains: 2
• Total formula weight: 96296.86

Authors

Ricagno, S.,Jonsson, S.,Richards, N.,Lindqvist, Y. (deposition date: 2003-04-28, release date: 2003-07-29, Last modification date: 2023-08-16)

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

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: 12839984
DOI: 10.1093/emboj/cdg333

Experimental method

X-RAY DIFFRACTION (2.5 Å)