› 2ol6

X-ray diffraction
1.6Å resolution

The crystal structure of OspA mutant

Released:
DOI: 10.2210/pdb2ol6/pdb
PDB entry 2ol6 coloured by chain, front view.
PDB entry 2ol6 coloured by chain, side view.
PDB entry 2ol6 coloured by chain, top view.
Source organism: Borreliella burgdorferi
Primary publication:
Beta-strand flipping and slipping triggered by turn replacement reveal the opportunistic nature of beta-strand pairing.
Makabe K, Yan S, Tereshko V, Gawlak G, Koide S
J Am Chem Soc 129 14661-9 (2007)
PMID: 17985889

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-175039 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer surface protein A Chain: O
Molecule details ›
Chain: O
Length: 250 amino acids
Theoretical weight: 26.25 KDa
Source organism: Borreliella burgdorferi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q45040 (Residues: 27-273; Coverage: 90%)
Gene name: 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: P21
Unit cell:
a: 32.882Å b: 51.508Å c: 65.639Å
α: 90° β: 98.56° γ: 90°
R-values:
R R work R free
0.22 0.218 0.259
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Fibrillar peptide gels in biotechnology and biomedicine.
Jung et al. (2010)
2 other articles

2 mentions without citation

Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.
Cieplak AS. (2017)
1 more