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


  • 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.

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

published in