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Formyl‐CoA transferase encloses the CoA binding site at the interface of an interlocked dimer
Author(s) -
Ricagno Stefano,
Jonsson Stefan,
Richards Nigel,
Lindqvist Ylva
Publication year - 2003
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/cdg333
Subject(s) - biology , transferase , dimer , binding site , genetics , biochemistry , microbiology and biotechnology , enzyme , physics , nuclear magnetic resonance
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 ∼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.