2VJQ

Formyl-CoA transferase mutant variant W48Q

Summary for 2VJQ

• Entry DOI: 10.2210/pdb2vjq/pdb
• Related: 1P5H 1P5R 1T3Z 1T4C 1VGQ 1VGR 2VJK 2VJL 2VJM 2VJN 2VJO 2VJP
• Descriptor: FORMYL-COENZYME A TRANSFERASE, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (3 entities in total)
• Functional Keywords: transferase, class iii coa transferase
• Biological source: OXALOBACTER FORMIGENES
• Cellular location: Cytoplasm: O06644
• Total number of polymer chains: 4
• Total formula weight: 189695.73

Authors

Toyota, C.G.,Berthold, C.L.,Gruez, A.,Jonsson, S.,Lindqvist, Y.,Cambillau, C.,Richards, N.G.J. (deposition date: 2007-12-11, release date: 2008-01-15, Last modification date: 2023-12-13)

Primary citation

Toyota, C.G.,Berthold, C.L.,Gruez, A.,Jonsson, S.,Lindqvist, Y.,Cambillau, C.,Richards, N.G.J.
Differential Substrate Specificity and Kinetic Behavior of Escherichia Coli Yfdw and Oxalobacter Formigenes Formyl Coenzyme a Transferase.
J.Bacteriol., 190:2556-, 2008

PubMed Abstract: The yfdXWUVE operon appears to encode proteins that enhance the ability of Escherichia coli MG1655 to survive under acidic conditions. Although the molecular mechanisms underlying this phenotypic behavior remain to be elucidated, findings from structural genomic studies have shown that the structure of YfdW, the protein encoded by the yfdW gene, is homologous to that of the enzyme that mediates oxalate catabolism in the obligate anaerobe Oxalobacter formigenes, O. formigenes formyl coenzyme A transferase (FRC). We now report the first detailed examination of the steady-state kinetic behavior and substrate specificity of recombinant, wild-type YfdW. Our studies confirm that YfdW is a formyl coenzyme A (formyl-CoA) transferase, and YfdW appears to be more stringent than the corresponding enzyme (FRC) in Oxalobacter in employing formyl-CoA and oxalate as substrates. We also report the effects of replacing Trp-48 in the FRC active site with the glutamine residue that occupies an equivalent position in the E. coli protein. The results of these experiments show that Trp-48 precludes oxalate binding to a site that mediates substrate inhibition for YfdW. In addition, the replacement of Trp-48 by Gln-48 yields an FRC variant for which oxalate-dependent substrate inhibition is modified to resemble that seen for YfdW. Our findings illustrate the utility of structural homology in assigning enzyme function and raise the question of whether oxalate catabolism takes place in E. coli upon the up-regulation of the yfdXWUVE operon under acidic conditions.

PubMed: 18245280
DOI: 10.1128/JB.01823-07

Experimental method

X-RAY DIFFRACTION (1.8 Å)