2bpq

From Proteopedia

Revision as of 14:40, 30 October 2007

ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE (TRPD) FROM MYCOBACTERIUM TUBERCULOSIS (APO STRUCTURE)

Overview

Mycobacterium tuberculosis, the cause of tuberculosis, presents a major, threat to human health worldwide. Biosynthetic enzymes that are essential, for the survival of the bacterium, especially in activated macrophages, are important potential drug targets. Although the tryptophan biosynthesis, pathway is thought to be non-essential for many pathogens, this appears, not to be the case for M.tuberculosis, where a trpD gene knockout fails to, cause disease in mice. We therefore chose the product of the trpD gene, anthranilate phosphoribosyltransferase, which catalyses the second step in, tryptophan biosynthesis, for structural analysis. The structure of TrpD, from M.tuberculosis was solved by X-ray crystallography, at 1.9 A, resolution for the native enzyme (R = 0.191, Rfree = 0.230) and at ... [(full description)]

About this Structure

2BPQ is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with BEN and GOL as [ligands]. Active as [Anthranilate phosphoribosyltransferase], with EC number [2.4.2.18]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate., Lee CE, Goodfellow C, Javid-Majd F, Baker EN, Shaun Lott J, J Mol Biol. 2006 Jan 27;355(4):784-97. Epub 2005 Nov 22. PMID:16337227

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