› 2v0l

X-ray diffraction
2.2Å resolution

Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-acetylglucosamine-1-phosphate Uridyltransferase (GlmU)

Released:
DOI: 10.2210/pdb2v0l/pdb
PDB entry 2v0l coloured by chain, front view.
PDB entry 2v0l coloured by chain, side view.
PDB entry 2v0l coloured by chain, top view.
Source organism: Haemophilus influenzae
Primary publication:
Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU).
Mochalkin I, Lightle S, Zhu Y, Ohren JF, Spessard C, Chirgadze NY, Banotai C, Melnick M, McDowell L
Protein Sci 16 2657-66 (2007)
PMID: 18029420

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 analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155145 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein GlmU Chain: A
Molecule details ›
Chain: A
Length: 456 amino acids
Theoretical weight: 49.35 KDa
Source organism: Haemophilus influenzae
UniProt:
  • Canonical: P43889 (Residues: 1-456; Coverage: 100%)
Gene names: HI_0642, glmU
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand URI 1 x URI
Ligand PG4 1 x PG4
Ligand PGE 2 x PGE
Ligand SO4 7 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: R32
Unit cell:
a: 108.72Å b: 108.72Å c: 326.754Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.187 not available

Quick links

Citations

2 review citations

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

2 mentions without citation

Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU).
Mochalkin et al. (2007)
1 more