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Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol- transfer protein

Author

Listed:
  • Bingdong Sha

    (Center for Macromolecular Crystallography)

  • Scott E. Phillips

    (University of Alabama at Birmingham)

  • Vytas A. Bankaitis

    (University of Alabama at Birmingham)

  • Ming Luo

    (Center for Macromolecular Crystallography)

Abstract

The yeast phosphatidylinositol-transfer protein (Sec14) catalyses exchange of phosphatidylinositol and phosphatidylcholine between membrane bilayers in vitro1,2. In vivo, Sec14 activity is essential for vesicle budding from the Golgi complex3. Here we report a three-dimensional structure for Sec14 at 2.5 Å resolution. Sec14 consists of twelve α-helices, six β-strands, eight 310-helices and has two distinct domains. The carboxy-terminal domain forms a hydrophobic pocket which, in the crystal ructure, is occupied by two molecules of n-octyl-β-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.

Suggested Citation

  • Bingdong Sha & Scott E. Phillips & Vytas A. Bankaitis & Ming Luo, 1998. "Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol- transfer protein," Nature, Nature, vol. 391(6666), pages 506-510, January.
    • Handle: RePEc:nat:nature:v:391:y:1998:i:6666:d:10.1038_35179
    DOI: 10.1038/35179
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    Cited by:

    1. Yunfeng Li & Yulia Pustovalova & Tzanko I. Doukov & Jeffrey C. Hoch & Richard E. Mains & Betty A. Eipper & Bing Hao, 2023. "Structure of the Sec14 domain of Kalirin reveals a distinct class of lipid-binding module in RhoGEFs," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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