1o6u
From Proteopedia
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==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 1O6U is a | + | 1O6U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PLM as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O6U OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:50:09 2007'' |
Revision as of 10:44, 5 November 2007
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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 with PLM as ligand. Structure known Active Site: AC1. 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
Page seeded by OCA on Mon Nov 5 12:50:09 2007
