› 1eeh

X-ray diffraction
1.9Å resolution

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

Released:
DOI: 10.2210/pdb1eeh/pdb
PDB entry 1eeh coloured by chain, front view.
PDB entry 1eeh coloured by chain, side view.
PDB entry 1eeh coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
"Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase.
Bertrand JA, Fanchon E, Martin L, Chantalat L, Auger G, Blanot D, van Heijenoort J, Dideberg O
J Mol Biol 301 1257-66 (2000)
PMID: 10966819

Function and Biology Details

Reaction catalysed: 
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147132 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylmuramoylalanine--D-glutamate ligase Chain: A
Molecule details ›
Chain: A
Length: 437 amino acids
Theoretical weight: 46.89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P14900 (Residues: 2-438; Coverage: 100%)
Gene names: JW0086, b0088, murD
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand UMA 1 x UMA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM02
Spacegroup: P212121
Unit cell:
a: 58.84Å b: 63.28Å c: 114.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.219 0.265
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Cytoplasmic steps of peptidoglycan biosynthesis.
Barreteau et al. (2008)
4 more

6 mentions without citation

Structural and functional features of enzymes of Mycobacterium tuberculosis peptidoglycan biosynthesis as targets for drug development.
Moraes et al. (2015)
5 more