4UAG

UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE

Summary for 4UAG

• Entry DOI: 10.2210/pdb4uag/pdb
• Descriptor: UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE, SULFATE ION, URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE-D-GLUTAMATE, ... (5 entities in total)
• Functional Keywords: ligase, peptidoglycan synthesis, murd, adp-forming enzyme
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 47907.93

Authors

Bertrand, J.,Auger, G.,Martin, L.,Fanchon, E.,Blanot, D.,Le Beller, D.,Van Heijenoort, J.,Dideberg, O. (deposition date: 1999-03-09, release date: 2000-03-15, Last modification date: 2023-12-27)

Primary citation

Bertrand, J.A.,Auger, G.,Martin, L.,Fanchon, E.,Blanot, D.,Le Beller, D.,van Heijenoort, J.,Dideberg, O.
Determination of the MurD mechanism through crystallographic analysis of enzyme complexes.
J.Mol.Biol., 289:579-590, 1999

PubMed 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.

PubMed: 10356330
DOI: 10.1006/jmbi.1999.2800

Experimental method

X-RAY DIFFRACTION (1.66 Å)