PMID:10356330
| Citation |
Bertrand, JA, Auger, G, Martin, L, Fanchon, E, Blanot, D, Le Beller, D, van Heijenoort, J and Dideberg, O (1999) Determination of the MurD mechanism through crystallographic analysis of enzyme complexes. J. Mol. Biol. 289:579-90 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1006/jmbi.1999.2800 |
| Keywords |
Adenosine Diphosphate/metabolism; Adenylyl Imidodiphosphate/chemistry; Adenylyl Imidodiphosphate/metabolism; Amino Acid Sequence; Crystallography, X-Ray; Dipeptides/chemistry; Dipeptides/metabolism; Hydrolysis; Magnesium/chemistry; Magnesium/metabolism; Manganese/chemistry; Manganese/metabolism; Models, Molecular; Molecular Sequence Data; Peptide Synthases/chemistry; Peptide Synthases/metabolism; Protein Conformation; Sequence Homology, Amino Acid; Uridine Diphosphate N-Acetylmuramic Acid/analogs & derivatives; Uridine Diphosphate N-Acetylmuramic Acid/chemistry; Uridine Diphosphate N-Acetylmuramic Acid/metabolism |
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