› 5a5e

X-ray diffraction
1.84Å resolution

CRYSTAL STRUCTURE OF MURD LIGASE FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb5a5e/pdb
PDB entry 5a5e coloured by chain, front view.
PDB entry 5a5e coloured by chain, side view.
PDB entry 5a5e coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Crystallographic Study of Peptidoglycan Biosynthesis Enzyme MurD: Domain Movement Revisited.
Šink R, Kotnik M, Zega A, Barreteau H, Gobec S, Blanot D, Dessen A, Contreras-Martel C
PLoS One 11 e0152075 (2016)
PMID: 27031227

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 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 K-12
Expression system: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: P14900 (Residues: 2-438; Coverage: 100%)
Gene names: JW0086, b0088, murD
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MPD 1 x MPD
Ligand NI 1 x NI
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 58.12Å b: 70.433Å c: 100.581Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.231
Expression system: Escherichia coli DH5[alpha]

Quick links

Citations

2 review citations

Structural conservation of the PIN domain active site across all domains of life.
Senissar et al. (2017)
1 more

3 mentions without citation

Crystallographic Study of Peptidoglycan Biosynthesis Enzyme MurD: Domain Movement Revisited.
Šink et al. (2016)
2 more