› 1f0k

X-ray diffraction
1.9Å resolution

THE 1.9 ANGSTROM CRYSTAL STRUCTURE OF E. COLI MURG

Released:
DOI: 10.2210/pdb1f0k/pdb
PDB entry 1f0k coloured by chain, front view.
PDB entry 1f0k coloured by chain, side view.
PDB entry 1f0k coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The 1.9 A crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis.
Ha S, Walker D, Shi Y, Walker S
Protein Sci 9 1045-52 (2000)
PMID: 10892798

Function and Biology Details

Reaction catalysed: 
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148068 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 364 amino acids
Theoretical weight: 39.06 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P17443 (Residues: 1-355; Coverage: 100%)
Gene names: JW0088, b0090, murG
Sequence domains:
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P1
Unit cell:
a: 60.613Å b: 66.356Å c: 67.902Å
α: 64.29° β: 83.52° γ: 65.45°
R-values:
R R work R free
0.22 0.22 0.247
Expression system: Escherichia coli

Quick links

Citations

30 review citations

Glycosyltransferases: structures, functions, and mechanisms.
Lairson et al. (2008)
29 more

22 mentions without citation

Structure-function relationships of membrane-associated GT-B glycosyltransferases.
Albesa-Jové et al. (2014)
21 more