› 1n2z

X-ray diffraction
2Å resolution

2.0 Angstrom structure of BtuF, the vitamin B12 binding protein of E. coli

Released:
DOI: 10.2210/pdb1n2z/pdb
PDB entry 1n2z coloured by chain, front view.
PDB entry 1n2z coloured by chain, side view.
PDB entry 1n2z coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter.
Borths EL, Locher KP, Lee AT, Rees DC
Proc Natl Acad Sci U S A 99 16642-7 (2002)
PMID: 12475936

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
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: 245 amino acids
Theoretical weight: 27.05 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P37028 (Residues: 22-266; Coverage: 100%)
Gene names: JW0154, b0158, btuF, yadT
Sequence domains: Periplasmic binding protein
Structure domains: Nitrogenase molybdenum iron protein domain

Ligands and Environments

4 bound ligands:
Ligand CD 22 x CD
Ligand CL 6 x CL
Ligand CNC 2 x CNC
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P65
Unit cell:
a: 133.066Å b: 133.066Å c: 67.687Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.189 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

37 review citations

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

10 mentions without citation

Bacterial heme-transport proteins and their heme-coordination modes.
Tong et al. (2009)
9 more