› 1oip

X-ray diffraction
1.95Å resolution

The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein

Released:
DOI: 10.2210/pdb1oip/pdb
PDB entry 1oip coloured by chain, front view.
PDB entry 1oip coloured by chain, side view.
PDB entry 1oip coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The molecular basis of vitamin E retention: structure of human alpha-tocopherol transfer protein.
Meier R, Tomizaki T, Schulze-Briese C, Baumann U, Stocker A
J Mol Biol 331 725-34 (2003)
PMID: 12899840

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155971 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-tocopherol transfer protein Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 31.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49638 (Residues: 1-278; Coverage: 100%)
Gene names: TPP1, TTPA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand VIV 1 x VIV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P41212
Unit cell:
a: 77.81Å b: 77.81Å c: 128.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.227
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

27 review citations

Vitamin E, antioxidant and nothing more.
Traber et al. (2007)
26 more

9 mentions without citation

Mechanisms of ligand transfer by the hepatic tocopherol transfer protein.
Morley et al. (2008)
8 more