1dss
From Proteopedia
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STRUCTURE OF ACTIVE-SITE CARBOXYMETHYLATED D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR
Overview
The structure of active site carboxymethylated, D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor was, determined in the presence of coenzyme NAD+ at 1.88 A resolution with a, final R-factor of 0.175. The structure refinement was carried out on the, basis of the structure of holo-GAPDH at 2.0 A resolution using the program, XPLOR. The carboxymethyl group connected to Cys149 is stabilized by a, hydrogen bond between its OZ1 and Cys149N, and charge interaction between, the carboxyl group and the nicotinamide moiety. The modification of Cys149, induced conformational changes in the active site, in particular, the site, of sulphate ion 501 (the proposed attacking inorganic phosphate ion in, catalysis), and segment 208-218 nearby. Extensive hydrogen-bonding, interactions ... [(full description)]
About this Structure
1DSS is a [Single protein] structure of sequence from [Palinurus versicolor] with SO4 and NAD as [ligands]. Active as [Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [1.2.1.12]. Structure known Active Sites: AVG and AVR. Full crystallographic information is available from [OCA].
Reference
Structure of active site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor., Song SY, Xu YB, Lin ZJ, Tsou CL, J Mol Biol. 1999 Apr 9;287(4):719-25. PMID:10191140
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