› 2b4m

X-ray diffraction
2.8Å resolution

Crystal structure of the binding protein OpuAC in complex with proline betaine

Released:
DOI: 10.2210/pdb2b4m/pdb
PDB entry 2b4m coloured by chain, front view.
PDB entry 2b4m coloured by chain, side view.
PDB entry 2b4m coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Molecular determinants for substrate specificity of the ligand-binding protein OpuAC from Bacillus subtilis for the compatible solutes glycine betaine and proline betaine.
Horn C, Sohn-Bösser L, Breed J, Welte W, Schmitt L, Bremer E
J Mol Biol 357 592-606 (2006)
PMID: 16445940

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155534 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine betaine-binding protein OpuAC Chains: A, B
Molecule details ›
Chains: A, B
Length: 268 amino acids
Theoretical weight: 29.78 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P46922 (Residues: 26-293; Coverage: 98%)
Gene names: BSU03000, opuAC
Sequence domains: Substrate binding domain of ABC-type glycine betaine transport system
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PBE 2 x PBE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21
Unit cell:
a: 88.562Å b: 28.318Å c: 102.826Å
α: 90° β: 93.87° γ: 90°
R-values:
R R work R free
0.233 0.231 0.283
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

A structural classification of substrate-binding proteins.
Berntsson et al. (2010)
5 more

1 mention without citation

The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies.
Smits et al. (2008)