1olm: Difference between revisions
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'''SUPERNATANT PROTEIN FACTOR IN COMPLEX WITH RRR-ALPHA-TOCOPHERYLQUINONE: A LINK BETWEEN OXIDIZED VITAMIN E AND CHOLESTEROL BIOSYNTHESIS''' | {{Structure | ||
|PDB= 1olm |SIZE=350|CAPTION= <scene name='initialview01'>1olm</scene>, resolution 1.95Å | |||
|SITE= <scene name='pdbsite=AC1:Vtq+Binding+Site+For+Chain+E'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=VTQ:RRR-ALPHA-TOCOPHERYLQUINONE'>VTQ</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SUPERNATANT PROTEIN FACTOR IN COMPLEX WITH RRR-ALPHA-TOCOPHERYLQUINONE: A LINK BETWEEN OXIDIZED VITAMIN E AND CHOLESTEROL BIOSYNTHESIS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1OLM is a [ | 1OLM is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLM OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12972248 12972248] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:12:27 2008'' | ||
Revision as of 11:12, 20 March 2008
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| 1olm, resolution 1.95Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | VTQ | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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 (RRR-alpha-TQ) in its protein body and permits a comparison with the recently solved structure of human alpha-tocopherol transfer protein (alpha-TTP) in complex with RRR-alpha-tocopherol. Recent findings have shown that RRR-alpha-TQ is reduced in vivo to RRR-alpha-TQH(2), the latter has been suggested to protect low-density lipoprotein (LDL) particles from oxidation. Hence, the antioxidant function of the redox couple RRR-alpha-TQ/RRR-alpha-TQH(2) in blocking LDL oxidation may reduce cellular cholesterol uptake and thus explain how SPF upregulates cholesterol synthesis.
About this Structure
1OLM is a Protein complex structure of sequences from Homo sapiens. 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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