› 1hm0

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE, GLMU

Released:
DOI: 10.2210/pdb1hm0/pdb
PDB entry 1hm0 coloured by chain, front view.
PDB entry 1hm0 coloured by chain, side view.
PDB entry 1hm0 coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture.
Sulzenbacher G, Gal L, Peneff C, Fassy F, Bourne Y
J Biol Chem 276 11844-51 (2001)
PMID: 11118459

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188962 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein GlmU Chains: A, B
Molecule details ›
Chains: A, B
Length: 468 amino acids
Theoretical weight: 50.54 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q97R46 (Residues: 2-459; Coverage: 100%)
Gene names: SP_0988, glmU
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: R3
Unit cell:
a: 92.715Å b: 92.715Å c: 280.387Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.207 0.244
Expression system: Escherichia coli

Quick links

Citations

10 review citations

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

2 mentions without citation

The structural biology of enzymes involved in natural product glycosylation.
Singh et al. (2012)
1 more