2ji6

From Proteopedia

Revision as of 09:43, 30 October 2007

X-RAY STRUCTURE OF OXALYL-COA DECARBOXYLASE IN COMPLEX WITH 3-DEAZA-THDP AND OXALYL-COA

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

2JI6 is a [Single protein] structure of sequence from [Oxalobacter formigenes] with MG, TPW, ADP, OXK, PGE and B3P 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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