› 3i3a

X-ray diffraction
2.12Å resolution

Structural Basis for the Sugar Nucleotide and Acyl Chain Selectivity of Leptospira interrogans LpxA

Released:
DOI: 10.2210/pdb3i3a/pdb
PDB entry 3i3a coloured by chain, front view.
PDB entry 3i3a coloured by chain, side view.
PDB entry 3i3a coloured by chain, top view.
Source organism: Leptospira interrogans
Primary publication:
Structural basis for the sugar nucleotide and acyl-chain selectivity of Leptospira interrogans LpxA.
Robins LI, Williams AH, Raetz CR
Biochemistry 48 6191-201 (2009)
PMID: 19456129

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184439 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP N-acetylglucosamine O-acyltransferase C-terminal domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 259 amino acids
Theoretical weight: 28.2 KDa
Source organism: Leptospira interrogans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8EZA6 (Residues: 1-259; Coverage: 100%)
Gene names: LA_3949, lpxA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand S2N 3 x S2N
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P321
Unit cell:
a: 108.155Å b: 108.155Å c: 116.886Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.213 0.269
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

3 mentions without citation

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