2c31
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(New page: 200px<br /> <applet load="2c31" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c31, resolution 1.73Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 16:51, 29 October 2007
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CRYSTAL STRUCTURE OF OXALYL-COA DECARBOXYLASE IN COMPLEX WITH THE COFACTOR DERIVATIVE THIAMIN-2-THIAZOLONE DIPHOSPHATE AND ADENOSINE DIPHOSPHATE
Overview
Oxalyl-coenzyme A decarboxylase is a thiamin diphosphate-dependent enzyme, that plays an important role in the catabolism of the highly toxic, compound oxalate. We have determined the crystal structure of the enzyme, from Oxalobacter formigenes from a hemihedrally twinned crystal to 1.73 A, resolution and characterized the steady-state kinetic behavior of the, decarboxylase. The monomer of the tetrameric enzyme consists of three, alpha/beta-type domains, commonly seen in this class of enzymes, and the, thiamin diphosphate-binding site is located at the expected, subunit-subunit interface between two of the domains with the cofactor, bound in the conserved V-conformation. Although oxalyl-CoA decarboxylase, is structurally homologous to acetohydroxyacid synthase, a molecule of ADP, is bound ... [(full description)]
About this Structure
2C31 is a [Single protein] structure of sequence from [Oxalobacter formigenes] with MG, TZD and ADP as [ligands]. Active as [[1]], with EC number [4.1.1.8]. Full crystallographic information is available from [OCA].
Reference
Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate., Berthold CL, Moussatche P, Richards NG, Lindqvist Y, J Biol Chem. 2005 Dec 16;280(50):41645-54. Epub 2005 Oct 10. PMID:16216870
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