1AUA

PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SEC14P FROM SACCHAROMYCES CEREVISIAE

Summary for 1AUA

• Entry DOI: 10.2210/pdb1aua/pdb
• Descriptor: PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SEC14P, octyl beta-D-glucopyranoside (3 entities in total)
• Functional Keywords: phospholipid-binding protein, peripheral golgi membrane protein, phospholipid exchange, golgi-derived secretory vesicle biogenesis
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 34630.32

Authors

Sha, B.,Phillips, S.E.,Bankaitis, V.A.,Luo, M. (deposition date: 1997-08-20, release date: 1997-12-24, Last modification date: 2024-02-07)

Primary citation

Sha, B.,Phillips, S.E.,Bankaitis, V.A.,Luo, M.
Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein.
Nature, 391:506-510, 1998

PubMed Abstract: 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.

PubMed: 9461221
DOI: 10.1038/35179

Experimental method

X-RAY DIFFRACTION (2.5 Å)