› 5lkw

X-ray diffraction
2Å resolution

Crystal structure of the peptidoglycan-associated lipoprotein (Pal) from Burkholderia cepacia in complex with DAP

Released:
DOI: 10.2210/pdb5lkw/pdb
PDB entry 5lkw coloured by chain, front view.
PDB entry 5lkw coloured by chain, side view.
PDB entry 5lkw coloured by chain, top view.
Source organism: Burkholderia cenocepacia J2315
Primary publication:
The Burkholderia cenocepacia peptidoglycan-associated lipoprotein is involved in epithelial cell attachment and elicitation of inflammation.
Dennehy R, Romano M, Ruggiero A, Mohamed YF, Dignam SL, Mujica Troncoso C, Callaghan M, Valvano MA, Berisio R, McClean S
Cell Microbiol 19 (2017)
PMID: 27886433

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110025 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidoglycan-associated lipoprotein Chains: A, B
Molecule details ›
Chains: A, B
Length: 130 amino acids
Theoretical weight: 14.91 KDa
Source organism: Burkholderia cenocepacia J2315
Expression system: Escherichia coli
UniProt:
  • Canonical: B4EDC1 (Residues: 51-170; Coverage: 80%)
Gene names: BCAL3204, pal
Sequence domains: OmpA family
Structure domains: OmpA-like domain

Ligands and Environments

1 bound ligand:
Ligand API 2 x API
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P32
Unit cell:
a: 77.706Å b: 77.706Å c: 38.606Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.188 0.249
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Bacterial lipids: powerful modifiers of the innate immune response.
Chandler et al. (2017)
4 more