› 5kn7

X-ray diffraction
1.99Å resolution

Lipid A secondary acyltransferase LpxM from Acinetobacter baumannii

Released:
DOI: 10.2210/pdb5kn7/pdb
PDB entry 5kn7 coloured by chain, front view.
PDB entry 5kn7 coloured by chain, side view.
PDB entry 5kn7 coloured by chain, top view.
Source organism: Acinetobacter baumannii NIPH 410
Primary publication:
Structure-guided enzymology of the lipid A acyltransferase LpxM reveals a dual activity mechanism.
Dovala D, Rath CM, Hu Q, Sawyer WS, Shia S, Elling RA, Knapp MS, Metzger LE
Proc Natl Acad Sci U S A 113 E6064-E6071 (2016)
PMID: 27681620

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-197409 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipid A biosynthesis lauroyl acyltransferase Chain: B
Molecule details ›
Chain: B
Length: 333 amino acids
Theoretical weight: 38.19 KDa
Source organism: Acinetobacter baumannii NIPH 410
Expression system: Escherichia coli

Ligands and Environments

5 bound ligands:
Ligand SO4 3 x SO4
Ligand NA 3 x NA
Ligand GOL 8 x GOL
Ligand LMT 1 x LMT
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2221
Unit cell:
a: 58.77Å b: 145.33Å c: 87.21Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.267
Expression system: Escherichia coli

Quick links

Citations

2 review citations

How lipid droplets "TAG" along: Glycerolipid synthetic enzymes and lipid storage.
Wang et al. (2017)
1 more

5 mentions without citation

Current Progress in the Structural and Biochemical Characterization of Proteins Involved in the Assembly of Lipopolysaccharide.
Bohl et al. (2018)
4 more