2ji8 | pdb_00002ji8

X-RAY STRUCTURE OF OXALYL-COA DECARBOXYLASE IN COMPLEX WITH FORMYL-COA

File:2ji8.jpg

spinqualitylabelsall models 2ji8, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

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 presented. In, accordance with mutagenesis data, no side chains of the enzyme are implied, to directly participate in proton transfer except the glutamic acid, (Glu-56), which promotes formation of the 1',4'-iminopyrimidine tautomer, of ThDP needed for activation.

About this Structure

2JI8 is a Single protein structure of sequence from Oxalobacter formigenes with MG, TPP, ADP, FYN and PGE as ligands. Active as Oxalyl-CoA decarboxylase, with EC number 4.1.1.8 Known structural/functional 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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