Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein. Academic Article

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.

authors

• Bankaitis, Vytas

published proceedings

• Nature

altmetric score

• 6

author list (cited authors)

• Sha, B., Phillips, S. E., Bankaitis, V. A., & Luo, M.

citation count

• 232

complete list of authors

• Sha, B||Phillips, SE||Bankaitis, VA||Luo, M

publication date

• January 1998

publisher

• Springer Nature  Publisher

published in

• Nature  Journal

keywords

• Carrier Proteins
• Crystallography, X-Ray
• Membrane Proteins
• Models, Molecular
• Phosphatidylinositols
• Phospholipid Transfer Proteins
• Protein Conformation
• Saccharomyces Cerevisiae
• Saccharomyces Cerevisiae Proteins

Digital Object Identifier (DOI)

• 10.1038/35179

start page

• 506

end page

• 510

volume

• 391

issue

• 6666

URL

• http://dx.doi.org/10.1038/35179