1szj

From Proteopedia

Revision as of 14:59, 5 November 2007

STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE FROM PALINURUS VERSICOLOR REFINED 2.0 ANGSTROM RESOLUTION

Overview

When the active-site carboxymethylated D-glyceraldehyde-3-phosphate, dehydrogenase is irradiated with ultraviolet light in the presence of, NAD+, a fluorescent NAD derivative that is covalently linked to the enzyme, is obtained. A preliminary crystallographic study of this fluorescent, derivative, as well as of the native and the carboxymethylated enzymes, from Palinurus versicolor, showed that they are isomorphous and belong to, space group C2 as reported for the native enzyme from Palinurus vulgaris., The three forms of the enzyme, although they have identical unit cell, parameters, differ considerably in their diffraction patterns, indicating, marked differences in conformation in spite of the fact that they differ, chemically only in a restricted region around the active site.

About this Structure

1SZJ 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 Site: ACT. Full crystallographic information is available from OCA.

Reference

Preliminary crystallographic studies of lobster D-glyceraldehyde-3-phosphate dehydrogenase and the modified enzyme carrying the fluorescent derivative., Song SY, Gao YG, Zhou JM, Tsou CL, J Mol Biol. 1983 Dec 5;171(2):225-8. PMID:6655693

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