3uag
UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
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OverviewOverview
UDP -N- acetylmuramoyl- L -alanine: D -glutamate (MurD) ligase catalyses, the addition of d -glutamate to the nucleotide precursor UDP -N-, acetylmuramoyl- L -alanine (UMA). The crystal structures of three, complexes of Escherichia coli MurD with a variety of substrates and, products have been determined to high resolution. These include (1) the, quaternary complex of MurD, the substrate UMA, the product ADP, and Mg2+, (2) the quaternary complex of MurD, the substrate UMA, the product ADP, and Mn2+, and (3) the binary complex of MurD with the product UDP - N-, acetylmuramoyl- L -alanine- D -glutamate (UMAG). The reaction mechanism, supported by these structures proceeds by the phosphorylation of the, C-terminal carboxylate group of UMA by the gamma-phosphate group of ATP to, form an acyl-phosphate intermediate, followed by the nucleophilic attack, by the amino group of D-glutamate to produce UMAG. A key feature in the, reaction intermediate is the presence of two magnesium ions bridging, negatively charged groups.
About this StructureAbout this Structure
3UAG is a Single protein structure of sequence from Escherichia coli with MN, UMA, ADP and EPE as ligands. Active as UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase, with EC number 6.3.2.9 Full crystallographic information is available from OCA.
ReferenceReference
Determination of the MurD mechanism through crystallographic analysis of enzyme complexes., Bertrand JA, Auger G, Martin L, Fanchon E, Blanot D, Le Beller D, van Heijenoort J, Dideberg O, J Mol Biol. 1999 Jun 11;289(3):579-90. PMID:10356330
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