1aua
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= SEC14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= SEC14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aua OCA], [http://www.ebi.ac.uk/pdbsum/1aua PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aua RCSB]</span> | ||
}} | }} | ||
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[[Category: Phillips, S E.]] | [[Category: Phillips, S E.]] | ||
[[Category: Sha, B.]] | [[Category: Sha, B.]] | ||
| - | [[Category: BOG]] | ||
[[Category: golgi-derived secretory vesicle biogenesis]] | [[Category: golgi-derived secretory vesicle biogenesis]] | ||
[[Category: peripheral golgi membrane protein]] | [[Category: peripheral golgi membrane protein]] | ||
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[[Category: phospholipid-binding protein]] | [[Category: phospholipid-binding protein]] | ||
| - | ''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 18:47:40 2008'' |
Revision as of 15:47, 30 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Gene: | SEC14 (Saccharomyces cerevisiae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SEC14P FROM SACCHAROMYCES CEREVISIAE
Overview
The yeast phosphatidylinositol-transfer protein (Sec14) catalyses exchange of phosphatidylinositol and phosphatidylcholine between membrane bilayers in vitro. In vivo, Sec14 activity is essential for vesicle budding from the Golgi complex. Here we report a three-dimensional structure for Sec14 at 2.5 A resolution. Sec14 consists of twelve alpha-helices, six beta-strands, eight 3(10)-helices and has two distinct domains. The carboxy-terminal domain forms a hydrophobic pocket which, in the crystal structure, is occupied by two molecules of n-octyl-beta-D-glucopyranoside and represents the phospholipid-binding domain. This pocket is reinforced by a string motif whose disruption in a sec14 temperature-sensitive mutant results in destabilization of the phospholipid-binding domain. Finally, we have identified an unusual surface helix that may play a critical role in driving Sec14-mediated phospholipid exchange. From this structure, we derive the first molecular clues into how a phosphatidylinositol-transfer protein functions.
About this Structure
1AUA is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein., Sha B, Phillips SE, Bankaitis VA, Luo M, Nature. 1998 Jan 29;391(6666):506-10. PMID:9461221
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