› 1oiz

X-ray diffraction
1.88Å resolution

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

Released:
DOI: 10.2210/pdb1oiz/pdb
PDB entry 1oiz coloured by chain, front view.
PDB entry 1oiz coloured by chain, side view.
PDB entry 1oiz 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 Chains: A, B
Molecule details ›
Chains: A, B
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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 45.144Å b: 113.775Å c: 67.433Å
α: 90° β: 98.95° γ: 90°
R-values:
R R work R free
0.197 0.195 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

26 review citations

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

6 mentions without citation

The Sec14 superfamily and mechanisms for crosstalk between lipid metabolism and lipid signaling.
Bankaitis et al. (2010)
5 more