1gr0

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Revision as of 14:07, 20 November 2007

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spinqualitylabelsall models 1gr0, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

MYO-INOSITOL 1-PHOSPHATE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH NAD AND ZINC.

Overview

Phosphatidylinositol (PI) is essential for Mycobacterium tuberculosis, viability and the enzymes involved in the PI biosynthetic pathway are, potential antimycobacterial agents for which little structural information, is available. The rate-limiting step in the pathway is the production of, (L)-myo-inositol 1-phosphate from (D)-glucose 6-phosphate, a complex, reaction catalyzed by the enzyme inositol 1-phosphate synthase. We have, determined the crystal structure of this enzyme from Mycobacterium, tuberculosis (tbINO) at 1.95 A resolution, bound to the cofactor NAD+. The, active site is located within a deep cleft at the junction between two, domains. The unexpected presence of a zinc ion here suggests a mechanistic, difference from the eukaryotic inositol synthases, which are stimulated by, monovalent cations, that may be exploitable in developing selective, inhibitors of tbINO.

About this Structure

1GR0 is a Single protein structure of sequence from Mycobacterium tuberculosis with ZN, CAC and NAD as ligands. Active as Inositol-3-phosphate synthase, with EC number 5.5.1.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of inositol 1-phosphate synthase from Mycobacterium tuberculosis, a key enzyme in phosphatidylinositol synthesis., Norman RA, McAlister MS, Murray-Rust J, Movahedzadeh F, Stoker NG, McDonald NQ, Structure. 2002 Mar;10(3):393-402. PMID:12005437

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