2KQ7

Solution structure of the Autophagy-Related Protein Atg8

2KQ7 の概要

• エントリーDOI: 10.2210/pdb2kq7/pdb
• 分子名称: Autophagy-related protein 8 (1 entity in total)
• 機能のキーワード: protein transport, autophagy, ubiquitin fold, cytoplasmic vesicle, lipoprotein, membrane, transport, ubl conjugation pathway, vacuole
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Cytoplasmic vesicle, cvt vesicle membrane; Lipid-anchor: P38182
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13792.94

構造登録者

Schwarten, M.,Stoldt, M.,Mohrluder, J.,Willbold, D. (登録日: 2009-10-29, 公開日: 2010-05-05, 最終更新日: 2024-05-29)

主引用文献

Schwarten, M.,Stoldt, M.,Mohrluder, J.,Willbold, D.
Solution structure of Atg8 reveals conformational polymorphism of the N-terminal domain
Biochem.Biophys.Res.Commun., 2010

PubMed Abstract: During autophagy a crescent shaped like membrane is formed, which engulfs the material that is to be degraded. This membrane grows further until its edges fuse to form the double membrane covered autophagosome. Atg8 is a protein, which is required for this initial step of autophagy. Therefore, a multistage conjugation process of newly synthesized Atg8 to phosphatidylethanolamine is of critical importance. Here we present the high resolution structure of unprocessed Atg8 determined by nuclear magnetic resonance spectroscopy. Its C-terminal subdomain shows a well-defined ubiquitin-like fold with slightly elevated mobility in the pico- to nanosecond timescale as determined by heteronuclear NOE data. In comparison to unprocessed Atg8, cleaved Atg8(G116) shows a decreased mobility behaviour. The N-terminal domain adopts different conformations within the micro- to millisecond timescale. The possible biological relevance of the differences in dynamic behaviours between both subdomains as well as between the cleaved and uncleaved forms is discussed.

PubMed: 20382112
DOI: 10.1016/j.bbrc.2010.04.043

実験手法

SOLUTION NMR