4EXV

Structure of Kluyveromyces lactis Hsv2p

4EXV の概要

• エントリーDOI: 10.2210/pdb4exv/pdb
• 分子名称: SVP1-like protein 2, SULFATE ION (2 entities in total)
• 機能のキーワード: proppin, wd-repeat, phosphoinosides, phosphatidylinositol, phosphate binding, autophagy, atg2, atg9, atg21, transport protein
• 由来する生物種: Kluyveromyces lactis (yeast)
• 細胞内の位置: Vacuole membrane; Peripheral membrane protein (By similarity): Q6CN23
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39508.13

構造登録者

Baskaran, S.,Hurley, J.H. (登録日: 2012-05-01, 公開日: 2012-07-04, 最終更新日: 2024-02-28)

主引用文献

Baskaran, S.,Ragusa, M.J.,Boura, E.,Hurley, J.H.
Two-Site Recognition of Phosphatidylinositol 3-Phosphate by PROPPINs in Autophagy.
Mol.Cell, 47:339-348, 2012

PubMed Abstract: Macroautophagy is essential to cell survival during starvation and proceeds by the growth of a double-membraned phagophore, which engulfs cytosol and other substrates. The synthesis and recognition of the lipid phosphatidylinositol 3-phosphate, PI(3)P, is essential for autophagy. The key autophagic PI(3)P sensors, which are conserved from yeast to humans, belong to the PROPPIN family. Here we report the crystal structure of the yeast PROPPIN Hsv2. The structure consists of a seven-bladed β-propeller and, unexpectedly, contains two pseudo-equivalent PI(3)P binding sites on blades 5 and 6. These two sites both contribute to membrane binding in vitro and are collectively required for full autophagic function in yeast. These sites function in concert with membrane binding by a hydrophobic loop in blade 6, explaining the specificity of the PROPPINs for membrane-bound PI(3)P. These observations thus provide a structural and mechanistic framework for one of the conserved central molecular recognition events in autophagy.

PubMed: 22704557
DOI: 10.1016/j.molcel.2012.05.027

実験手法

X-RAY DIFFRACTION (3 Å)