1e0d
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UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
OverviewOverview
UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (MurD) is a cytoplasmic, enzyme involved in the biosynthesis of peptidoglycan which catalyzes the, addition of D-glutamate to the nucleotide precursor, UDP-N-acetylmuramoyl-L-alanine (UMA). The crystal structure of MurD in the, presence of its substrate UMA has been solved to 1.9 A resolution. Phase, information was obtained from multiple anomalous dispersion using the, K-shell edge of selenium in combination with multiple isomorphous, replacement. The structure comprises three domains of topology each, reminiscent of nucleotide-binding folds: the N- and C-terminal domains are, consistent with the dinucleotide-binding fold called the Rossmann fold, and the central domain with the mononucleotide-binding fold also observed, in the GTPase family. The structure reveals the binding site of the, substrate UMA, and comparison with known NTP complexes allows the, identification of residues interacting with ATP. The study describes the, first structure of the UDP-N-acetylmuramoyl-peptide ligase family.
About this StructureAbout this Structure
1E0D is a Single protein structure of sequence from Escherichia coli with SO4 as ligand. 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
Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli., Bertrand JA, Auger G, Fanchon E, Martin L, Blanot D, van Heijenoort J, Dideberg O, EMBO J. 1997 Jun 16;16(12):3416-25. PMID:9218784
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