1KCM

Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms Resolution

1KCM の概要

• エントリーDOI: 10.2210/pdb1kcm/pdb
• 関連するPDBエントリー: 1FVZ
• 分子名称: Phosphatidylinositol Transfer Protein alpha (2 entities in total)
• 機能のキーワード: pitp, phospholipid binding protein, phospholipid transport, lipid binding protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm: P53810
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31810.23

構造登録者

Schouten, A.,Agianian, B.,Westerman, J.,Kroon, J.,Wirtz, K.W.A.,Gros, P. (登録日: 2001-11-09, 公開日: 2002-05-08, 最終更新日: 2023-08-16)

主引用文献

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

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: 11980708
DOI: 10.1093/emboj/21.9.2117

実験手法

X-RAY DIFFRACTION (2 Å)