
Structure of autophagy‐related protein Atg8 from the silkworm Bombyx mori
Author(s) -
Hu Chen,
Zhang Xuan,
Teng YanBin,
Hu HaiXi,
Li WeiFang
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110018464
Subject(s) - atg8 , bombyx mori , autophagy , ubiquitin , microbiology and biotechnology , chemistry , n terminus , biology , biochemistry , peptide sequence , gene , apoptosis
Autophagy‐related protein Atg8 is ubiquitous in all eukaryotes. It is involved in the Atg8–PE ubiquitin‐like conjugation system, which is essential for autophagosome formation. The structures of Atg8 from different species are very similar and share a ubiquitin‐fold domain at the C‐terminus. In the 2.40 Å crystal structure of Atg8 from the silkworm Bombyx mori reported here, the ubiquitin fold at the C‐terminus is preceded by two additional helices at the N‐terminus.