1KCM
Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms Resolution
Summary for 1KCM
| Entry DOI | 10.2210/pdb1kcm/pdb |
| Related | 1FVZ |
| Descriptor | Phosphatidylinositol Transfer Protein alpha (2 entities in total) |
| Functional Keywords | pitp, phospholipid binding protein, phospholipid transport, lipid binding protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm: P53810 |
| Total number of polymer chains | 1 |
| Total formula weight | 31810.23 |
| Authors | Schouten, A.,Agianian, B.,Westerman, J.,Kroon, J.,Wirtz, K.W.A.,Gros, P. (deposition date: 2001-11-09, release date: 2002-05-08, Last modification date: 2023-08-16) |
| Primary citation | Schouten, A.,Agianian, B.,Westerman, J.,Kroon, J.,Wirtz, K.W.,Gros, P. Structure of apo-phosphatidylinositol transfer protein alpha provides insight into membrane association. EMBO J., 21:2117-2121, 2002 Cited by PubMed Abstract: Phosphatidylinositol transfer protein alpha (PITP alpha) is a ubiquitous and highly conserved protein in multicellular eukaryotes that catalyzes the exchange of phospholipids between membranes in vitro and participates in cellular phospholipid metabolism, signal transduction and vesicular trafficking in vivo. Here we report the three-dimensional crystal structure of a phospholipid-free mouse PITP alpha at 2.0 A resolution. The structure reveals an open conformation characterized by a channel running through the protein. The channel is created by opening the phospholipid-binding cavity on one side by displacement of the C-terminal region and a hydrophobic lipid exchange loop, and on the other side by flattening of the central beta-sheet. The relaxed conformation is stabilized at the proposed membrane association site by hydrophobic interactions with a crystallographically related molecule, creating an intimate dimer. The observed open conformer is consistent with a membrane-bound state of PITP and suggests a mechanism for membrane anchoring and the presentation of phosphatidylinositol to kinases and phospholipases after its extraction from the membrane. Coordinates have been deposited in the Protein Data Bank (accession No. 1KCM). PubMed: 11980708DOI: 10.1093/emboj/21.9.2117 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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