› 1y9u

X-ray diffraction
1.39Å resolution

Bordetella ferric binding protein

Released:
DOI: 10.2210/pdb1y9u/pdb
PDB entry 1y9u coloured by chain, front view.
PDB entry 1y9u coloured by chain, side view.
PDB entry 1y9u coloured by chain, top view.
Source organism: Bordetella pertussis Tohama I
Primary publication:
Anion-independent iron coordination by the Campylobacter jejuni ferric binding protein.
Tom-Yew SA, Cui DT, Bekker EG, Murphy ME
J Biol Chem 280 9283-90 (2005)
PMID: 15613474

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182089 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Iron binding protein Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 34.82 KDa
Source organism: Bordetella pertussis Tohama I
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7VXW9 (Residues: 31-349; Coverage: 100%)
Gene name: BP1605
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL
Spacegroup: P212121
Unit cell:
a: 59.39Å b: 71.47Å c: 74.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.184
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Coordination chemistry of bacterial metal transport and sensing.
Ma et al. (2009)
4 more

2 mentions without citation

Photolysis of iron-siderophore chelates promotes bacterial-algal mutualism.
Amin et al. (2009)
1 more