1h3m

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[[Category: synthetase]]
[[Category: synthetase]]
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Revision as of 14:22, 5 November 2007


1h3m, resolution 2.40Å

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STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2C-METHYL-D-ERYTHRITOL SYNTHETASE

Overview

2-C-Methyl-D-erythritol 4-phosphate cytidylyltransferase is an essential, enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis., The structure of a tetragonal crystal form has been solved by molecular, replacement and refined to 2.4 A resolution. Structure and sequence, comparisons suggest that the enzyme is a suitable target for a, structure-based approach to the development of novel broad-spectrum, antibiotics. However, the absence of ligands in the enzyme active site, together with the moderate resolution of the structure indicates that this, tetragonal crystal form is inferior to that of a previously reported, highly ordered monoclinic form [Richard et al. (2001), Nature Struct., Biol. 8, 641-647].

About this Structure

1H3M is a Single protein structure of sequence from Escherichia coli with CL and N2P as ligands. Active as 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, with EC number 2.7.7.60 Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase., Kemp LE, Bond CS, Hunter WN, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):607-10. Epub 2003, Feb 21. PMID:12595740

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