2jib

From Proteopedia

Revision as of 09:42, 30 October 2007

X-RAY STRUCTURE OF OXALYL-COA DECARBOXYLASE IN COMPLEX WITH COENZYME-A

Overview

Despite more than five decades of extensive studies of thiamin diphosphate, (ThDP) enzymes, there remain many uncertainties as to how these enzymes, achieve their rate enhancements. Here, we present a clear picture of, catalysis for the simple nonoxidative decarboxylase, oxalyl-coenzyme A, (CoA) decarboxylase, based on crystallographic snapshots along the, catalytic cycle and kinetic data on active site mutants. First, we provide, crystallographic evidence that, upon binding of oxalyl-CoA, the C-terminal, 13 residues fold over the substrate, aligning the substrate alpha-carbon, for attack by the ThDP-C2 atom. The second structure presented shows a, covalent reaction intermediate after decarboxylation, interpreted as being, nonplanar. Finally, the structure of a product complex is ... [(full description)]

About this Structure

2JIB is a [Single protein] structure of sequence from [Oxalobacter formigenes] with MG, COA, TPP, ADP and PGE as [ligands]. Active as [Oxalyl-CoA decarboxylase], with EC number [4.1.1.8]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases., Berthold CL, Toyota CG, Moussatche P, Wood MD, Leeper F, Richards NG, Lindqvist Y, Structure. 2007 Jul;15(7):853-61. PMID:17637344

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