1o6u: Difference between revisions
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|PDB= 1o6u |SIZE=350|CAPTION= <scene name='initialview01'>1o6u</scene>, resolution 2.05Å | |PDB= 1o6u |SIZE=350|CAPTION= <scene name='initialview01'>1o6u</scene>, resolution 2.05Å | ||
|SITE= <scene name='pdbsite=AC1:Plm+Binding+Site+For+Chain+E'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Plm+Binding+Site+For+Chain+E'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=PLM:PALMITIC ACID'>PLM</scene> | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6u OCA], [http://www.ebi.ac.uk/pdbsum/1o6u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o6u RCSB]</span> | |||
}} | }} | ||
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[[Category: Stocker, A.]] | [[Category: Stocker, A.]] | ||
[[Category: Tomizaki, T.]] | [[Category: Tomizaki, T.]] | ||
[[Category: cral_trio]] | [[Category: cral_trio]] | ||
[[Category: lipid binding]] | [[Category: lipid binding]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:40:41 2008'' | ||
Revision as of 19:40, 30 March 2008
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| 1o6u, resolution 2.05Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | MSE, PLM | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
THE CRYSTAL STRUCTURE OF HUMAN SUPERNATANT PROTEIN FACTOR
Overview
Supernatant protein factor (SPF) promotes the epoxidation of squalene catalyzed by microsomes. Several studies suggest its in vivo role in the cholesterol biosynthetic pathway by a yet unknown mechanism. SPF belongs to a family of lipid binding proteins called CRAL_TRIO, which include yeast phosphatidylinositol transfer protein Sec14 and tocopherol transfer protein TTP. The crystal structure of human SPF at a resolution of 1.9 A reveals a two domain topology. The N-terminal 275 residues form a Sec14-like domain, while the C-terminal 115 residues consist of an eight-stranded jelly-roll barrel similar to that found in many viral protein structures. The ligand binding cavity has a peculiar horseshoe-like shape. Contrary to the Sec14 crystal structure, the lipid-exchange loop is in a closed conformation, suggesting a mechanism for lipid exchange.
About this Structure
1O6U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the human supernatant protein factor., Stocker A, Tomizaki T, Schulze-Briese C, Baumann U, Structure. 2002 Nov;10(11):1533-40. PMID:12429094
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