Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8

Title
Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8
Authors
홍승범김병원이경은김세웅전혜성김준송현규
Issue Date
2011-12
Publisher
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Citation
VOL 18, NO 12, 1323-1330
Abstract
Autophagy is the degradation of cellular organelles via the lysosomal pathway. The autophagic ubiquitin-like (Ubl) molecule Atg8 is activated by the E1-like enzyme Atg7. As this noncanonical E1 enzyme’s domain organization is unique among Ubl-activating E1 enzymes, the structural basis for its interactions with Atg8 and partner E2 enzymes remains obscure. Here we present the structure of the N-terminal domain of Atg7, revealing a unique protein fold and interactions with both autophagic E2 enzymes Atg3 and Atg10. The structure of the C-terminal domain of Atg7 in complex with Atg8 shows the mode of dimerization and mechanism of recognition of Atg8. Notably, the catalytic cysteine residue in Atg7 is positioned close to the C-terminal glycine of Atg8, its target for thioester formation, potentially eliminating the need for large conformational rearrangements characteristic of other E1s.
URI
http://pubs.kist.re.kr/handle/201004/42571
ISSN
1545-9985
Appears in Collections:
KIST Publication > Article
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE