5DFZ

Structure of Vps34 complex II from S. cerevisiae.

5DFZ の概要

• エントリーDOI: 10.2210/pdb5dfz/pdb
• 分子名称: Vacuolar protein sorting-associated protein 38, Phosphatidylinositol 3-kinase VPS34, Serine/threonine-protein kinase VPS15, ... (6 entities in total)
• 機能のキーワード: vps34, vps15, vps30, vps38, autophagy, vacuolar protein sorting, yeast, complex ii, pi3p, kinase, lipid, wd40, bara, c2, coiled-coil, heat, nanobody, transferase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• 細胞内の位置: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q05919 P22543; Golgi apparatus, trans-Golgi network membrane; Lipid-anchor: P22219; Endosome membrane; Peripheral membrane protein: Q02948
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 400489.65

構造登録者

Rostislavleva, K.,Soler, N.,Ohashi, Y.,Zhang, L.,Williams, R.L. (登録日: 2015-08-27, 公開日: 2015-10-07, 最終更新日: 2024-05-08)

主引用文献

Rostislavleva, K.,Soler, N.,Ohashi, Y.,Zhang, L.,Pardon, E.,Burke, J.E.,Masson, G.R.,Johnson, C.,Steyaert, J.,Ktistakis, N.T.,Williams, R.L.
Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes.
Science, 350:aac7365-aac7365, 2015

PubMed Abstract: Phosphatidylinositol 3-kinase Vps34 complexes regulate intracellular membrane trafficking in endocytic sorting, cytokinesis, and autophagy. We present the 4.4 angstrom crystal structure of the 385-kilodalton endosomal complex II (PIK3C3-CII), consisting of Vps34, Vps15 (p150), Vps30/Atg6 (Beclin 1), and Vps38 (UVRAG). The subunits form a Y-shaped complex, centered on the Vps34 C2 domain. Vps34 and Vps15 intertwine in one arm, where the Vps15 kinase domain engages the Vps34 activation loop to regulate its activity. Vps30 and Vps38 form the other arm that brackets the Vps15/Vps34 heterodimer, suggesting a path for complex assembly. We used hydrogen-deuterium exchange mass spectrometry (HDX-MS) to reveal conformational changes accompanying membrane binding and identify a Vps30 loop that is critical for the ability of complex II to phosphorylate giant liposomes on which complex I is inactive.

PubMed: 26450213
DOI: 10.1126/science.aac7365

実験手法

X-RAY DIFFRACTION (4.4 Å)