Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer.

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 an

SUBMITTER: Ricagno S 

PROVIDER: S-EPMC165657 | biostudies-literature | 2003 Jul

REPOSITORIES: biostudies-literature