1gl3

From Proteopedia

Revision as of 13:09, 30 October 2007

ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE IN COMPLEX WITH NADP AND SUBSTRATE ANALOGUE S-METHYL CYSTEINE SULFOXIDE

Overview

Aspartate-beta-semialdehyde dehydrogenase (ASADH) lies at the first branch, point in the biosynthetic pathway through which bacteria, fungi, and the, higher plants synthesize amino acids, including lysine and methionine and, the cell wall component diaminopimelate from aspartate. Blocks in this, biosynthetic pathway, which is absent in mammals, are lethal, and, inhibitors of ASADH may therefore serve as useful antibacterial, fungicidal, or herbicidal agents. We have determined the structure of, ASADH from Escherichia coli by crystallography in the presence of its, coenzyme and a substrate analogue that acts as a covalent inhibitor. This, structure is comparable to that of the covalent intermediate that forms, during the reaction catalyzed by ASADH. The key catalytic residues are, ... [(full description)]

About this Structure

1GL3 is a [Single protein] structure of sequence from [Escherichia coli] with CYS and NDP as [ligands]. Active as [Aspartate-semialdehyde dehydrogenase], with EC number [1.2.1.11]. Structure known Active Site: AT1. Full crystallographic information is available from [OCA].

Reference

Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase., Hadfield A, Shammas C, Kryger G, Ringe D, Petsko GA, Ouyang J, Viola RE, Biochemistry. 2001 Dec 4;40(48):14475-83. PMID:11724560

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