› 2wsx

X-ray diffraction
3.5Å resolution

Crystal Structure of Carnitine Transporter from Escherichia coli

Released:
DOI: 10.2210/pdb2wsx/pdb
PDB entry 2wsx coloured by chain, front view.
PDB entry 2wsx coloured by chain, side view.
PDB entry 2wsx coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT.
Schulze S, Köster S, Geldmacher U, Terwisscha van Scheltinga AC, Kühlbrandt W
Nature 467 233-6 (2010)
PMID: 20829798

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-152034 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-carnitine/gamma-butyrobetaine antiporter Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 504 amino acids
Theoretical weight: 56.64 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P31553 (Residues: 1-504; Coverage: 100%)
Gene names: JW0039, b0040, caiT, yaaP
Sequence domains: BCCT, betaine/carnitine/choline family transporter

Ligands and Environments

1 bound ligand:
Ligand NM2 6 x NM2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P32
Unit cell:
a: 124.2Å b: 124.2Å c: 154.63Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.237 0.271

Quick links

Citations

14 review citations

SLC6 neurotransmitter transporters: structure, function, and regulation.
Kristensen et al. (2011)
13 more

8 mentions without citation

Alternating access mechanisms of LeuT-fold transporters: trailblazing towards the promised energy landscapes.
Kazmier et al. (2017)
7 more