Structure of a multifunctional protein - Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine
Abstract
Eukaryotic phosphatidylinositol transfer protein is a ubiquitous multifunctional protein that transports phospholipids between membrane surfaces and participates in cellular phospholipid metabolism during signal transduction and vesicular trafficking. The three-dimensional structure of the α-isoform of rat phosphatidylinositol transfer protein complexed with one molecule of phosphatidylcholine, one of its physiological ligands, has been determined to 2.2 Å resolution by x-ray diffraction techniques. A single ß -sheet and several long α-helices define an enclosed internal cavity in which a single molecule of the phospholipid is accommodated with its polar head group in the center of the protein and fatty acyl chains projected toward the surface. Other structural features suggest mechanisms by which cytosolic phosphatidylinositol transfer protein interacts with membranes for lipid exchange and associates with a variety of lipid and protein kinases.
Additional Information
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc. Received for publication, November 7, 2000, and in revised form, November 27, 2000. Published, JBC Papers in Press, December 4, 2000, DOI 10.1074/jbc.M010131200 The atomic coordinates for the crystal structure of PITPα·PtdCho have been deposited in the Research Collaboratory for Structural Bioinformatics Protein Data Bank with accession code 1FVZ. We thank Chuong Doan and Sienna Sifuentes for technical assistance. Diffraction data for this study were collected at Brookhaven National Laboratory in the Biology Department single-crystal diffraction facility at beamline X12-C in the National Synchrotron Light Source. This facility is supported by the United States Department of Energy Offices of Health and Environmental Research and of Basic Energy Sciences under prime contract DE-AC02-98CH10886, by the National Science Foundation and by National Institutes of Health Grant 1P41 RR12408-01A1. We are grateful for the assistance of Michael Becker and Robert Sweet with "Fed-Ex Data Collection" at X12-C. This work was supported by National Institutes of Health Grants GM24035 (to G.M.H. and L.R.Y.) and GM59162 (to G.M.H., L.R.Y., and M.D.Y.), the American Heart Association (to L.R.Y.), and the University of Kansas Medical Center Research Institute (to G.M.H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.Files
| Name | Size | Download all |
|---|---|---|
|
md5:875f50ba629453eb9b01c41a38e1cda5
|
3.2 MB | Preview Download |
Additional details
- Eprint ID
- 5322
- Resolver ID
- CaltechAUTHORS:YODjbc01
- Created
-
2006-10-10Created from EPrint's datestamp field
- Updated
-
2021-11-08Created from EPrint's last_modified field