› 4pz5

X-ray diffraction
1.96Å resolution

Crystal structure of the second and third fibronectin F1 modules in complex with a fragment of BBK32 from Borrelia burgdorferi

Released:
DOI: 10.2210/pdb4pz5/pdb
PDB entry 4pz5 coloured by chain, front view.
PDB entry 4pz5 coloured by chain, side view.
PDB entry 4pz5 coloured by chain, top view.
Source organisms:
Primary publication:
Borrelia burgdorferi protein BBK32 binds to soluble fibronectin via the N-terminal 70-kDa region, causing fibronectin to undergo conformational extension.
Harris G, Ma W, Maurer LM, Potts JR, Mosher DF
J Biol Chem 289 22490-9 (2014)
PMID: 24962582

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129339 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Fibronectin Chain: A
Molecule details ›
Chain: A
Length: 90 amino acids
Theoretical weight: 10.12 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P02751 (Residues: 93-182; Coverage: 4%)
Gene names: FN, FN1
Sequence domains: Fibronectin type I domain
Structure domains: Complement Module, domain 1
Fibronectin-binding protein BBK32 Chain: B
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.86 KDa
Source organism: Borreliella burgdorferi B31
Expression system: Not provided
UniProt:
  • Canonical: O50835 (Residues: 175-189; Coverage: 4%)
Gene names: BB_K32, bbk32

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P6522
Unit cell:
a: 86.58Å b: 86.58Å c: 63.57Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.163 0.161 0.199
Expression systems:
  • Komagataella pastoris
  • Not provided

Quick links

Citations

3 review citations

Dynamic structure of plasma fibronectin.
Maurer et al. (2015)
2 more

2 mentions without citation

Interaction with the host: the role of fibronectin and extracellular matrix proteins in the adhesion of Gram-negative bacteria.
Vaca et al. (2020)
1 more