› 5n2c

X-ray diffraction
1.8Å resolution

Crystal structure of the peptidoglycan-associated lipoprotein from Burkholderia cenocepacia

Released:
DOI: 10.2210/pdb5n2c/pdb
PDB entry 5n2c coloured by chain, front view.
PDB entry 5n2c coloured by chain, side view.
PDB entry 5n2c coloured by chain, top view.
Source organism: Burkholderia cenocepacia J2315
Primary publication:
Designing Probes for Immunodiagnostics: Structural Insights into an Epitope Targeting Burkholderia Infections.
Capelli R, Matterazzo E, Amabili M, Peri C, Gori A, Gagni P, Chiari M, Lertmemongkolchai G, Cretich M, Bolognesi M, Colombo G, Gourlay LJ
ACS Infect Dis 3 736-743 (2017)
PMID: 28707874

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110026 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidoglycan-associated lipoprotein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 185 amino acids
Theoretical weight: 20.57 KDa
Source organism: Burkholderia cenocepacia J2315
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B4EDC1 (Residues: 19-170; Coverage: 100%)
Gene names: BCAL3204, pal
Sequence domains: OmpA family
Structure domains: OmpA-like domain

Ligands and Environments

4 bound ligands:
Ligand EDO 5 x EDO
Ligand CXS 3 x CXS
Ligand OXL 3 x OXL
Ligand ACT 4 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2221
Unit cell:
a: 70.433Å b: 104.532Å c: 110.436Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.219
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Postgenomic Approaches and Bioinformatics Tools to Advance the Development of Vaccines against Bacteria of the Burkholderia cepacia Complex.
Sousa et al. (2018)
1 more