6IYY

Crystal structure of human WIPI3,loop deletion mutant

6IYY の概要

• エントリーDOI: 10.2210/pdb6iyy/pdb
• 分子名称: WD repeat domain phosphoinositide-interacting protein 3, SULFATE ION (3 entities in total)
• 機能のキーワード: membrane bound protein, lipid binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35639.44

構造登録者

Liang, R.B.,Ren, J.Q.,Feng, W. (登録日: 2018-12-17, 公開日: 2019-03-13, 最終更新日: 2024-03-27)

主引用文献

Liang, R.,Ren, J.,Zhang, Y.,Feng, W.
Structural Conservation of the Two Phosphoinositide-Binding Sites in WIPI Proteins.
J. Mol. Biol., 431:1494-1505, 2019

PubMed Abstract: WIPI proteins are mammalian PROPPIN family members that bind to phosphoinositides and play prominent roles in autophagosome biogenesis. Two phosphoinositide-binding sites were previously described in yeast PROPPIN Hsv2 but remain to be determined in mammalian WIPI proteins. Here, we characterized four human WIPI proteins (WIPI1-4) and solved the structure of WIPI3. WIPI proteins can bind to PI(3)P and PI(3,5)P and adopt a conventional seven-bladed β-propeller fold. The structure of WIPI3 revealed that WIPI proteins also contain two sites embedded in blades 5 and 6 for recognizing phosphoinositides, resembling that in Hsv2. Structural comparison further demonstrated that the two conserved phosphoinositide-binding sites in PROPPIN proteins are not identical but intrinsically tend to recognize different types of phosphoinositides. This work provides the structural evidence to support the conservation of the two phosphoinositide-binding sites in WIPI proteins and also uncovers the potential phosphoinositide-binding selectivity for each site.

PubMed: 30797857
DOI: 10.1016/j.jmb.2019.02.019

実験手法

X-RAY DIFFRACTION (1.796 Å)