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X-ray diffraction
3.35Å resolution

CRYSTAL STRUCTURE OF THE SODIUM-COUPLED GLYCINE BETAINE SYMPORTER BETP FROM CORYNEBACTERIUM GLUTAMICUM WITH BOUND SUBSTRATE

Released:
DOI: 10.2210/pdb2wit/pdb
PDB entry 2wit coloured by chain, front view.
PDB entry 2wit coloured by chain, side view.
PDB entry 2wit coloured by chain, top view.
Source organism: Corynebacterium glutamicum
Primary publication:
Molecular basis of transport and regulation in the Na(+)/betaine symporter BetP.
Ressl S, Terwisscha van Scheltinga AC, Vonrhein C, Ott V, Ziegler C
Nature 458 47-52 (2009)
PMID: 19262666

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: 61.71 KDa
Source organism: Corynebacterium glutamicum
Expression system: Escherichia coli BL21
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

1 bound ligand:
Ligand BET 3 x BET
1 modified residue:
Ligand MSE 45 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 118.095Å b: 129.422Å c: 182.942Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.257 0.257 0.265
Expression system: Escherichia coli BL21

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Citations

51 review citations

Biology of human sodium glucose transporters.
Wright et al. (2011)
50 more

14 mentions without citation

Bacterial responses to osmotic challenges.
Wood JM. (2015)
13 more