› 2aq9

X-ray diffraction
1.8Å resolution

Structure of E. coli LpxA with a bound peptide that is competitive with acyl-ACP

Released:
DOI: 10.2210/pdb2aq9/pdb
PDB entry 2aq9 coloured by chain, front view.
PDB entry 2aq9 coloured by chain, side view.
PDB entry 2aq9 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structure of UDP-N-acetylglucosamine acyltransferase with a bound antibacterial pentadecapeptide.
Williams AH, Immormino RM, Gewirth DT, Raetz CR
Proc Natl Acad Sci U S A 103 10877-82 (2006)
PMID: 16835299

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:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141515 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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:
peptide inhibitor Chain: X
Molecule details ›
Chain: X
Length: 15 amino acids
Theoretical weight: 1.69 KDa
Source organism: Escherichia coli K-12
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand PO4 5 x PO4
Ligand DMS 22 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P213
Unit cell:
a: 96.734Å b: 96.734Å c: 96.734Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.226
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

8 review citations

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

8 mentions without citation

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