1fxj
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(New page: 200px<br /><applet load="1fxj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fxj, resolution 2.25Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 13:19, 20 November 2007
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CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE
Overview
N-acetylglucosamine 1-phosphate uridyltransferase (GlmU) is a cytoplasmic, bifunctional enzyme involved in the biosynthesis of the, nucleotide-activated UDP-GlcNAc, which is an essential precursor for the, biosynthetic pathways of peptidoglycan and other components in bacteria., The crystal structure of a truncated form of GlmU has been solved at 2.25, A resolution using the multiwavelength anomalous dispersion technique and, its function tested with mutagenesis studies. The molecule is composed of, two distinct domains connected by a long alpha-helical arm: (i) an, N-terminal domain which resembles the dinucleotide-binding Rossmann fold;, and (ii) a C-terminal domain which adopts a left-handed parallel, beta-helix structure (LbetaH) as found in homologous bacterial, acetyltransferases. Three GlmU molecules assemble into a trimeric, arrangement with tightly packed parallel LbetaH domains, the long, alpha-helical linkers being seated on top of the arrangement and the, N-terminal domains projected away from the 3-fold axis. In addition, the, 2.3 A resolution structure of the GlmU-UDP-GlcNAc complex reveals the, structural bases required for the uridyltransferase activity. These, structures exemplify a three-dimensional template for the development of, new antibacterial agents and for studying other members of the large, family of XDP-sugar bacterial pyrophosphorylases.
About this Structure
1FXJ is a Single protein structure of sequence from Escherichia coli with SO4 and MES as ligands. Active as UDP-N-acetylglucosamine diphosphorylase, with EC number 2.7.7.23 Full crystallographic information is available from OCA.
Reference
Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily., Brown K, Pompeo F, Dixon S, Mengin-Lecreulx D, Cambillau C, Bourne Y, EMBO J. 1999 Aug 2;18(15):4096-107. PMID:10428949
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