4UAG: Udp-N-Acetylmuramoyl-L-Alanine:d-Glutamate Ligase

Citation:
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.
PDB ID: 4UAGDownload
MMDB ID: 13019
PDB Deposition Date: 1999/3/9
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 1.66  Å
Source Organism:
Similar Structures:
Biological Unit for 4UAG: monomeric; determined by author
Molecular Components in 4UAG
Label Count Molecule
Protein (1 molecule)
1
Udp-n-acetylmuramoyl-l-alanine:d-glutamate Ligase(Gene symbol: murD)
Molecule annotation
Chemicals (10 molecules)
1
1
2
1
3
8
Molecule information is not avaliable.
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.