1aua: Difference between revisions

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[[Image:1aua.gif|left|200px]]
[[Image:1aua.gif|left|200px]]


{{Structure
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The line below this paragraph, containing "STRUCTURE_1aua", creates the "Structure Box" on the page.
|SITE=
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|GENE= SEC14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
{{STRUCTURE_1aua| PDB=1aua  | SCENE= }}  
|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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'''PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SEC14P FROM SACCHAROMYCES CEREVISIAE'''
'''PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SEC14P FROM SACCHAROMYCES CEREVISIAE'''
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[[Category: Phillips, S E.]]
[[Category: Phillips, S E.]]
[[Category: Sha, B.]]
[[Category: Sha, B.]]
[[Category: golgi-derived secretory vesicle biogenesis]]
[[Category: Golgi-derived secretory vesicle biogenesis]]
[[Category: peripheral golgi membrane protein]]
[[Category: Peripheral golgi membrane protein]]
[[Category: phospholipid exchange]]
[[Category: Phospholipid exchange]]
[[Category: phospholipid-binding protein]]
[[Category: Phospholipid-binding protein]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:47:40 2008''

Revision as of 10:42, 2 May 2008

File:1aua.gif

Template:STRUCTURE 1aua

PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SEC14P FROM SACCHAROMYCES CEREVISIAE


OverviewOverview

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 StructureAbout this Structure

1AUA is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Fri May 2 10:41:59 2008

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