› 2qia

X-ray diffraction
1.74Å resolution

Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine Acyltransferase

Released:
DOI: 10.2210/pdb2qia/pdb
PDB entry 2qia coloured by chain, front view.
PDB entry 2qia coloured by chain, side view.
PDB entry 2qia coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase.
Williams AH, Raetz CR
Proc Natl Acad Sci U S A 104 13543-50 (2007)
PMID: 17698807

Function and Biology Details

Reaction catalysed: 
A (3R)-3-hydroxyacyl-[acyl-carrier-protein] + UDP-N-acetyl-alpha-D-glucosamine = an [acyl-carrier-protein] + a UDP-3-O-(3-hydroxyacylyl)-N-acetyl-alpha-D-glucosamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141513 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 28.12 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A722 (Residues: 1-262; Coverage: 100%)
Gene names: JW0176, b0181, lpxA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand U20 1 x U20
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P213
Unit cell:
a: 97.143Å b: 97.143Å c: 97.143Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.232
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Biosynthesis and export of bacterial lipopolysaccharides.
Whitfield et al. (2014)
7 more

11 mentions without citation

Structure, inhibition, and regulation of essential lipid A enzymes.
Zhou et al. (2017)
10 more