1ep0

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Revision as of 20:31, 24 November 2007

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spinqualitylabelsall models 1ep0, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HIGH RESOLUTION CRYSTAL STRUCTURE OF DTDP-6-DEOXY-D-XYLO-4-HEXULOSE 3,5-EPIMERASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

Overview

Deoxythymidine diphosphate (dTDP)-4-keto-6-deoxy-d-hexulose 3, 5-epimerase, (RmlC) is involved in the biosynthesis of dTDP-l-rhamnose, which is an, essential component of the bacterial cell wall. The crystal structure of, RmlC from Methanobacterium thermoautotrophicum was determined in the, presence and absence of dTDP, a substrate analogue. RmlC is a homodimer, comprising a central jelly roll motif, which extends in two directions, into longer beta-sheets. Binding of dTDP is stabilized by ionic, interactions to the phosphate group and by a combination of ionic and, hydrophobic interactions with the base. The active site, which is located, in the center of the jelly roll, is formed by residues that are conserved, in all known RmlC sequence homologues. The conservation of the active site, residues suggests that the mechanism of action is also conserved and that, the RmlC structure may be useful in guiding the design of antibacterial, drugs.

About this Structure

1EP0 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Active as dTDP-4-dehydrorhamnose 3,5-epimerase, with EC number 5.1.3.13 Full crystallographic information is available from OCA.

Reference

Crystal structure of dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase from Methanobacterium thermoautotrophicum complexed with dTDP., Christendat D, Saridakis V, Dharamsi A, Bochkarev A, Pai EF, Arrowsmith CH, Edwards AM, J Biol Chem. 2000 Aug 11;275(32):24608-12. PMID:10827167

Page seeded by OCA on Sat Nov 24 22:38:48 2007