1aua
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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 with BOG as ligand. 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
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