› 2rej

X-ray diffraction
2.6Å resolution

ABC-transporter choline binding protein in unliganded semi-closed conformation

Released:
DOI: 10.2210/pdb2rej/pdb
PDB entry 2rej coloured by chain, front view.
PDB entry 2rej coloured by chain, side view.
PDB entry 2rej coloured by chain, top view.
Source organism: Sinorhizobium meliloti
Primary publication:
Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states.
Oswald C, Smits SH, Höing M, Sohn-Bösser L, Dupont L, Le Rudulier D, Schmitt L, Bremer E
J Biol Chem 283 32848-59 (2008)
PMID: 18779321

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-571799 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ABC-type glycine betaine transport system substrate-binding domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 298 amino acids
Theoretical weight: 32.3 KDa
Source organism: Sinorhizobium meliloti
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92N37 (Residues: 28-318; Coverage: 100%)
Gene names: SMc02737, choX
Sequence domains: Substrate binding domain of ABC-type glycine betaine transport system
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P21
Unit cell:
a: 34.1Å b: 232.5Å c: 47.3Å
α: 90° β: 90.2° γ: 90°
R-values:
R R work R free
0.299 0.296 0.359
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.
Eitinger et al. (2011)
1 more

1 mention without citation

Quantitatively characterizing the ligand binding mechanisms of choline binding protein using Markov state model analysis.
Gu et al. (2014)