› 4doj

X-ray diffraction
3.25Å resolution

Crystal structure of BetP in outward-facing conformation

Released:
DOI: 10.2210/pdb4doj/pdb
PDB entry 4doj coloured by chain, front view.
PDB entry 4doj coloured by chain, side view.
PDB entry 4doj coloured by chain, top view.
Source organism: Corynebacterium glutamicum
Primary publication:
Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP.
Perez C, Koshy C, Yildiz O, Ziegler C
Nature 490 126-30 (2012)
PMID: 22940865

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157051 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine betaine transporter BetP Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 566 amino acids
Theoretical weight: 61.23 KDa
Source organism: Corynebacterium glutamicum
Expression system: Escherichia coli
UniProt:
  • Canonical: P54582 (Residues: 30-595; Coverage: 95%)
Gene names: Cgl0892, betP, cg1016
Sequence domains: BCCT, betaine/carnitine/choline family transporter
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

3 bound ligands:
Ligand CL 2 x CL
Ligand PGT 1 x PGT
Ligand CHT 1 x CHT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 117.44Å b: 129.32Å c: 184.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.254 0.249 0.297
Expression system: Escherichia coli

Quick links

Citations

21 review citations

Shared Molecular Mechanisms of Membrane Transporters.
Drew et al. (2016)
20 more

7 mentions without citation

The Role of the Membrane in Transporter Folding and Activity.
Ernst et al. (2021)
6 more