› 3eh0

X-ray diffraction
2.6Å resolution

Crystal Structure of LpxD from Escherichia coli

Released:
DOI: 10.2210/pdb3eh0/pdb
PDB entry 3eh0 coloured by chain, front view.
PDB entry 3eh0 coloured by chain, side view.
PDB entry 3eh0 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis.
Bartling CM, Raetz CR
Biochemistry 48 8672-83 (2009)
PMID: 19655786

Function and Biology Details

Reaction catalysed: 
A (3R)-3-hydroxyacyl-[acyl-carrier-protein] + a UDP-3-O-((3R)-hydroxyacyl)-alpha-D-glucosamine = a UDP-2-N,3-O-bis((3R)-3-hydroxyacyl)-alpha-D-glucosamine + a holo-[acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149339 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 341 amino acids
Theoretical weight: 36.05 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P21645 (Residues: 1-341; Coverage: 100%)
Gene names: JW0174, b0179, firA, lpxD, omsA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 157.95Å b: 94.17Å c: 103.66Å
α: 90° β: 126.5° γ: 90°
R-values:
R R work R free
0.217 0.214 0.279
Expression system: Escherichia coli

Quick links

Citations

10 review citations

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

8 mentions without citation

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