› 1j2z

X-ray diffraction
2.1Å resolution

Crystal structure of UDP-N-acetylglucosamine acyltransferase

Released:
DOI: 10.2210/pdb1j2z/pdb
PDB entry 1j2z coloured by chain, front view.
PDB entry 1j2z coloured by chain, side view.
PDB entry 1j2z coloured by chain, top view.
Source organism: Helicobacter pylori
Primary publication:
Crystal structure of UDP-N-acetylglucosamine acyltransferase from Helicobacter pylori.
Lee BI, Suh SW
Proteins 53 772-4 (2003)
PMID: 14579368

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

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-518904 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase Chain: A
Molecule details ›
Chain: A
Length: 270 amino acids
Theoretical weight: 29.9 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli
UniProt:
  • Canonical: O25927 (Residues: 1-270; Coverage: 100%)
Gene names: HP_1375, lpxA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand SOG 1 x SOG
Ligand SO4 2 x SO4
Ligand TLA 1 x TLA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P6322
Unit cell:
a: 90.686Å b: 90.686Å c: 148.203Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.222 0.222 0.264
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Lipid A modification systems in gram-negative bacteria.
Raetz et al. (2007)
3 more

6 mentions without citation

Repeat-protein folding: new insights into origins of cooperativity, stability, and topology.
Kloss et al. (2008)
5 more