› 1hv9

X-ray diffraction
2.1Å resolution

STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES

Released:
DOI: 10.2210/pdb1hv9/pdb
PDB entry 1hv9 coloured by chain, front view.
PDB entry 1hv9 coloured by chain, side view.
PDB entry 1hv9 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.
Olsen LR, Roderick SL
Biochemistry 40 1913-21 (2001)
PMID: 11329257

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-142259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein GlmU Chains: A, B
Molecule details ›
Chains: A, B
Length: 456 amino acids
Theoretical weight: 49.25 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0ACC7 (Residues: 1-456; Coverage: 100%)
Gene names: JW3708, b3730, glmU, yieA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand COA 2 x COA
2 bound ligands:
Ligand CO 5 x CO
Ligand UD1 2 x UD1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: R32
Unit cell:
a: 104.5Å b: 104.5Å c: 648.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.211 0.248
Expression system: Escherichia coli BL21

Quick links

Citations

14 review citations

Lipopolysaccharide endotoxins.
Raetz et al. (2002)
13 more

12 mentions without citation

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