3VU4

Crystal structure of Kluyvelomyces marxianus Hsv2

3VU4 の概要

• エントリーDOI: 10.2210/pdb3vu4/pdb
• 分子名称: KmHsv2, SULFATE ION (3 entities in total)
• 機能のキーワード: beta-propeller fold, protein transport
• 由来する生物種: Kluyveromyces marxianus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 83155.10

構造登録者

Watanabe, Y.,Noda, N.N. (登録日: 2012-06-15, 公開日: 2012-07-04, 最終更新日: 2024-03-20)

主引用文献

Watanabe, Y.,Kobayashi, T.,Yamamoto, H.,Hoshida, H.,Akada, R.,Inagaki, F.,Ohsumi, Y.,Noda, N.N.
Structure-based analyses reveal distinct binding sites for Atg2 and phosphoinositides in Atg18.
J.Biol.Chem., 287:31681-31690, 2012

PubMed Abstract: Autophagy is an intracellular degradation system by which cytoplasmic materials are enclosed by an autophagosome and delivered to a lysosome/vacuole. Atg18 plays a critical role in autophagosome formation as a complex with Atg2 and phosphatidylinositol 3-phosphate (PtdIns(3)P). However, little is known about the structure of Atg18 and its recognition mode of Atg2 or PtdIns(3)P. Here, we report the crystal structure of Kluyveromyces marxianus Hsv2, an Atg18 paralog, at 2.6 Å resolution. The structure reveals a seven-bladed β-propeller without circular permutation. Mutational analyses of Atg18 based on the K. marxianus Hsv2 structure suggested that Atg18 has two phosphoinositide-binding sites at blades 5 and 6, whereas the Atg2-binding region is located at blade 2. Point mutations in the loops of blade 2 specifically abrogated autophagy without affecting another Atg18 function, the regulation of vacuolar morphology at the vacuolar membrane. This architecture enables Atg18 to form a complex with Atg2 and PtdIns(3)P in parallel, thereby functioning in the formation of autophagosomes at autophagic membranes.

PubMed: 22851171
DOI: 10.1074/jbc.M112.397570

実験手法

X-RAY DIFFRACTION (2.6 Å)