› 2oy7

X-ray diffraction
1.55Å resolution

The crystal structure of OspA mutant

Released:
DOI: 10.2210/pdb2oy7/pdb
PDB entry 2oy7 coloured by chain, front view.
PDB entry 2oy7 coloured by chain, side view.
PDB entry 2oy7 coloured by chain, top view.
Source organism: Borreliella burgdorferi
Primary publication:
Aromatic cross-strand ladders control the structure and stability of beta-rich peptide self-assembly mimics.
Biancalana M, Makabe K, Koide A, Koide S
J Mol Biol 383 205-13 (2008)
PMID: 18762191

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-143538 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer surface protein A Chain: A
Molecule details ›
Chain: A
Length: 320 amino acids
Theoretical weight: 34.67 KDa
Source organism: Borreliella burgdorferi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CL66 (Residues: 27-122, 123-273; Coverage: 96%)
Gene names: BB_A15, ospA
Sequence domains: Borrelia lipoprotein
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 37.055Å b: 93.103Å c: 106.101Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.191 0.22
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Molecular mechanism of Thioflavin-T binding to amyloid fibrils.
Biancalana et al. (2010)
5 more

5 mentions without citation

Protein Design: From the Aspect of Water Solubility and Stability.
Qing et al. (2022)
4 more