› 4b2f

X-ray diffraction
1.88Å resolution

N-terminal deletion mutant of an outer surface protein BBA73 from Borrelia burgdorferi

Released:
DOI: 10.2210/pdb4b2f/pdb
PDB entry 4b2f coloured by chain, front view.
PDB entry 4b2f coloured by chain, side view.
PDB entry 4b2f coloured by chain, top view.
Source organism: Borreliella burgdorferi B31
Primary publication:
Structural characterization of the Borrelia burgdorferi outer surface protein BBA73 implicates dimerization as a functional mechanism.
Brangulis K, Petrovskis I, Kazaks A, Baumanis V, Tars K
Biochem Biophys Res Commun 434 848-53 (2013)
PMID: 23618869

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129345 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Antigen P35 Chain: A
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 24.9 KDa
Source organism: Borreliella burgdorferi B31
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O50962 (Residues: 87-296; Coverage: 78%)
Gene name: BB_A73
Sequence domains: Borrelia Bbcrasp-1 domain containing protein
Structure domains: Bbcrasp-1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P43212
Unit cell:
a: 74.34Å b: 74.34Å c: 95.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.205 0.235
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The surface lipoproteins of gram-negative bacteria: Protectors and foragers in harsh environments.
Cole et al. (2021)
2 other articles

1 mention without citation

Structural and Functional Analysis of BBA03, Borrelia burgdorferi Competitive Advantage Promoting Outer Surface Lipoprotein.
Fridmanis et al. (2020)