› 2jf2

X-ray diffraction
1.8Å resolution

Nucleotide substrate binding by UDP-N-acetylglucosamine acyltransferase

Released:
DOI: 10.2210/pdb2jf2/pdb
PDB entry 2jf2 coloured by chain, front view.
PDB entry 2jf2 coloured by chain, side view.
PDB entry 2jf2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Nucleotide substrate recognition by UDP-N-acetylglucosamine acyltransferase (LpxA) in the first step of lipid A biosynthesis.
Ulaganathan V, Buetow L, Hunter WN
J Mol Biol 369 305-12 (2007)
PMID: 17434525

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: 264 amino acids
Theoretical weight: 28.26 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A722 (Residues: 1-262; Coverage: 100%)
Gene names: JW0176, b0181, lpxA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PEG 1 x PEG
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P213
Unit cell:
a: 95.402Å b: 95.402Å c: 95.402Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.163 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Current Progress in the Structural and Biochemical Characterization of Proteins Involved in the Assembly of Lipopolysaccharide.
Bohl et al. (2018)
16 other articles

2 mentions without citation

A rapid coarse residue-based computational method for x-ray solution scattering characterization of protein folds and multiple conformational states of large protein complexes.
Yang et al. (2009)
1 more