› 1n4a

X-ray diffraction
2Å resolution

The Ligand Bound Structure of E.coli BtuF, the Periplasmic Binding Protein for Vitamin B12

Released:
DOI: 10.2210/pdb1n4a/pdb
PDB entry 1n4a coloured by chain, front view.
PDB entry 1n4a coloured by chain, side view.
PDB entry 1n4a coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding.
Karpowich NK, Huang HH, Smith PC, Hunt JF
J Biol Chem 278 8429-34 (2003)
PMID: 12468528

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153331 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vitamin B12-binding protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 252 amino acids
Theoretical weight: 28.14 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P37028 (Residues: 23-266; Coverage: 100%)
Gene names: JW0154, b0158, btuF, yadT
Sequence domains: Periplasmic binding protein
Structure domains: Nitrogenase molybdenum iron protein domain

Ligands and Environments

1 bound ligand:
Ligand CNC 2 x CNC
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P21212
Unit cell:
a: 131.73Å b: 92.02Å c: 44.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.234 0.261
Expression system: Escherichia coli BL21(DE3)

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Citations

29 review citations

Structure, function, and evolution of bacterial ATP-binding cassette systems.
Davidson et al. (2008)
28 more

11 mentions without citation

Characterization of a Bacillus subtilis transporter for petrobactin, an anthrax stealth siderophore.
Zawadzka et al. (2009)
10 more