1T27

THE STRUCTURE OF PITP COMPLEXED TO PHOSPHATIDYLCHOLINE

Replaces:  1FVZ

Summary for 1T27

• Entry DOI: 10.2210/pdb1t27/pdb
• Descriptor: Phosphatidylinositol transfer protein alpha isoform, 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total)
• Functional Keywords: lipid binding protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: P16446
• Total number of polymer chains: 1
• Total formula weight: 32742.57

Authors

Yoder, M.D.,Thomas, L.M.,Tremblay, J.M.,Oliver, R.L.,Yarbrough, L.R.,Helmkamp Jr., G.M. (deposition date: 2004-04-20, release date: 2004-05-11, Last modification date: 2024-02-14)

Primary citation

Yoder, M.D.,Thomas, L.M.,Tremblay, J.M.,Oliver, R.L.,Yarbrough, L.R.,Helmkamp Jr., G.M.
STRUCTURE OF A MULTIFUNCTIONAL PROTEIN. MAMMALIAN PHOSPHATIDYLINOSITOL TRANSFER PROTEIN COMPLEXED WITH PHOSPHATIDYLCHOLINE
J.Biol.Chem., 276:9246-9252, 2001

PubMed 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 alpha-isoform of rat phosphatidylinositol transfer protein complexed with one molecule of phosphatidylcholine, one of its physiological ligands, has been determined to 2.2 A resolution by x-ray diffraction techniques. A single beta-sheet and several long alpha-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.

PubMed: 11104777
DOI: 10.1074/jbc.M010131200

Experimental method

X-RAY DIFFRACTION (2.2 Å)