› 2jff

X-ray diffraction
1.89Å resolution

Crystal structure of MurD ligase in complex with D-Glu containing sulfonamide inhibitor

Released:
DOI: 10.2210/pdb2jff/pdb
PDB entry 2jff coloured by chain, front view.
PDB entry 2jff coloured by chain, side view.
PDB entry 2jff coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase.
Kotnik M, Humljan J, Contreras-Martel C, Oblak M, Kristan K, Hervé M, Blanot D, Urleb U, Gobec S, Dessen A, Solmajer T
J Mol Biol 370 107-15 (2007)
PMID: 17507028

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: 445 amino acids
Theoretical weight: 47.98 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: P14900 (Residues: 1-438; Coverage: 100%)
Gene names: JW0086, b0088, murD
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand LK2 1 x LK2
Ligand SO4 2 x SO4
1 modified residue:
Ligand KCX 1 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P41
Unit cell:
a: 65.288Å b: 65.288Å c: 135.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.215
Expression system: Escherichia coli DH5[alpha]

Quick links

Citations

9 review citations

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

5 mentions without citation

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