1x0x

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(New page: 200px<br /> <applet load="1x0x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x0x, resolution 2.75Å" /> '''Co-Structure of Hom...)
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Revision as of 17:51, 12 November 2007

Image:1x0x.gif

Co-Structure of Homo Sapiens Glycerol-3-Phosphate Dehydrogenase 1 complex with NAD

Overview

Homo sapiens L-alpha-glycerol-3-phosphate dehydrogenase 1 (GPD1) catalyzes, the reversible biological conversion of dihydroxyacetone (DHAP) to, glycerol-3-phosphate. The GPD1 protein was expressed in Escherichia coli, and purified as a fusion protein with glutathione S-transferase. Here we, report the apoenzyme structure of GPD1 determined by multiwavelength, anomalous diffraction phasing, and other complex structures with small, molecules (NAD+ and DHAP) by the molecular replacement method. This enzyme, structure is organized into two distinct domains, the N-terminal, eight-stranded beta-sheet sandwich domain and the C-terminal helical, substrate-binding domain. An electrophilic catalytic mechanism by the, epsilon-NH3+ group of Lys204 is proposed on the basis of the structural, analyses. In addition, the inhibitory effects of zinc and sulfate on GPDHs, are assayed and discussed.

About this Structure

1X0X is a Single protein structure of sequence from Homo sapiens with SO4 and NAD as ligands. Active as Glycerol-3-phosphate dehydrogenase (NAD(+)), with EC number 1.1.1.8 Full crystallographic information is available from OCA.

Reference

Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1)., Ou X, Ji C, Han X, Zhao X, Li X, Mao Y, Wong LL, Bartlam M, Rao Z, J Mol Biol. 2006 Mar 31;357(3):858-69. Epub 2006 Jan 18. PMID:16460752

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