1olm | pdb_00001olm
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SUPERNATANT PROTEIN FACTOR IN COMPLEX WITH RRR-ALPHA-TOCOPHERYLQUINONE: A LINK BETWEEN OXIDIZED VITAMIN E AND CHOLESTEROL BIOSYNTHESIS
Overview
The vast majority of monomeric lipid transport in nature is performed by, lipid-specific protein carriers. This class of proteins can enclose, cognate lipid molecules in a hydrophobic cavity and transport them across, the aqueous environment. Supernatant protein factor (SPF) is an enigmatic, representative of monomeric lipid transporters belonging to the SEC14, family. SPF stimulates squalene epoxidation, a downstream step of the, cholesterol biosynthetic pathway, by an unknown mechanism. Here, we, present the three-dimensional crystal structure of human SPF in complex, with RRR-alpha-tocopherylquinone, the major physiological oxidation, product of RRR-alpha-tocopherol, at a resolution of 1.95A. The structure, of the complex reveals how SPF sequesters RRR-alpha-tocopherylquinone, ... [(full description)]
About this Structure
1OLM is a [Protein complex] structure of sequences from [Homo sapiens] with VTQ as [ligand]. Full crystallographic information is available from [OCA].
Reference
Supernatant protein factor in complex with RRR-alpha-tocopherylquinone: a link between oxidized Vitamin E and cholesterol biosynthesis., Stocker A, Baumann U, J Mol Biol. 2003 Sep 26;332(4):759-65. PMID:12972248
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