1gx1

From Proteopedia

Revision as of 13:17, 30 October 2007

STRUCTURE OF 2C-METHYL-D-ERYTHRITOL-2,4-CYCLODIPHOSPHATE SYNTHASE

Overview

The crystal structure of the zinc enzyme Escherichia coli, 2C-methyl-d-erythritol 2,4-cyclodiphosphate synthase in complex with, cytidine 5'-diphosphate and Mn(2+) has been determined to 1.8-A, resolution. This enzyme is essential in E. coli and participates in the, nonmevalonate pathway of isoprenoid biosynthesis, a critical pathway, present in some bacterial and apicomplexans but distinct from that used by, mammals. Our analysis reveals a homotrimer, built around a beta prism, carrying three active sites, each of which is formed in a cleft between, pairs of subunits. Residues from two subunits recognize and bind the, nucleotide in an active site that contains a Zn(2+) with tetrahedral, coordination. A Mn(2+), with octahedral geometry, is positioned between, the alpha and beta phosphates ... [(full description)]

About this Structure

1GX1 is a [Single protein] structure of sequence from [Escherichia coli] with ZN, MN, SO4 and CDF as [ligands]. Active as [2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase], with EC number [4.6.1.12]. Structure known Active Site: CA1. Full crystallographic information is available from [OCA].

Reference

Structure of 2C-methyl-D-erythritol 2,4- cyclodiphosphate synthase: an essential enzyme for isoprenoid biosynthesis and target for antimicrobial drug development., Kemp LE, Bond CS, Hunter WN, Proc Natl Acad Sci U S A. 2002 May 14;99(10):6591-6. Epub 2002 May 7. PMID:11997478

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