2KQ7

Solution structure of the Autophagy-Related Protein Atg8

Summary for 2KQ7

• Entry DOI: 10.2210/pdb2kq7/pdb
• Descriptor: Autophagy-related protein 8 (1 entity in total)
• Functional Keywords: protein transport, autophagy, ubiquitin fold, cytoplasmic vesicle, lipoprotein, membrane, transport, ubl conjugation pathway, vacuole
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Cytoplasmic vesicle, cvt vesicle membrane; Lipid-anchor: P38182
• Total number of polymer chains: 1
• Total formula weight: 13792.94

Authors

Schwarten, M.,Stoldt, M.,Mohrluder, J.,Willbold, D. (deposition date: 2009-10-29, release date: 2010-05-05, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

SOLUTION NMR