› 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 1oip coloured by chain and viewed from the front.
PDB 1oip coloured by chain and viewed from the side.
PDB 1oip coloured by chain and viewed from the top.
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)
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
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)

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Citations

24 review citations

Utilization of Vitamin E Analogs to Protect Normal Tissues While Enhancing Antitumor Effects.
Aykin-Burns et al. (2019)
23 more

8 mentions without citation

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