› 1yh8

X-ray diffraction
2.7Å resolution

Crystal structure of Aquifex aeolicus LpxC deacetylase complexed with palmitate

Released:
DOI: 10.2210/pdb1yh8/pdb
PDB entry 1yh8 coloured by chain, front view.
PDB entry 1yh8 coloured by chain, side view.
PDB entry 1yh8 coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism.
Hernick M, Gennadios HA, Whittington DA, Rusche KM, Christianson DW, Fierke CA
J Biol Chem 280 16969-78 (2005)
PMID: 15705580

Function and Biology Details

Reaction catalysed: 
UDP-3-O-((3R)-3-hydroxyacyl)-N-acetyl-alpha-D-glucosamine + H(2)O = UDP-3-O-((3R)-3-hydroxyacyl)-alpha-D-glucosamine + acetate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130527 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-3-O-acyl-N-acetylglucosamine deacetylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 270 amino acids
Theoretical weight: 30.86 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O67648 (Residues: 2-271; Coverage: 96%)
Gene names: aq_1772, envA, lpxC
Sequence domains: UDP-3-O-acyl N-acetylglycosamine deacetylase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 5 x ZN
Ligand CL 3 x CL
Ligand PAM 2 x PAM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P61
Unit cell:
a: 101.61Å b: 101.61Å c: 124.18Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.201 0.239
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

1 mention without citation

Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase.
Gennadios et al. (2006)