| Literature DB >> 28945247 |
Yusuke Sato1,2,3,4, Kei Okatsu1,2,4, Yasushi Saeki5, Koji Yamano5, Noriyuki Matsuda5,6, Ai Kaiho5, Atsushi Yamagata1,2,3,4, Sakurako Goto-Ito1,2,3,4, Minoru Ishikawa7, Yuichi Hashimoto7, Keiji Tanaka5, Shuya Fukai1,2,3,4.
Abstract
Parkin ubiquitin (Ub) ligase (also known as PARK2) ubiquitinates damaged mitochondria for their clearance and quality control. USP30 deubiquitinase opposes parkin-mediated Ub-chain formation on mitochondria by preferentially cleaving Lys6-linked Ub chains. Here, we report the crystal structure of zebrafish USP30 in complex with a Lys6-linked diubiquitin (diUb or Ub2) at 1.87-Å resolution. The distal Ub-recognition mechanism of USP30 is similar to those of other USP family members, whereas Phe4 and Thr12 of the proximal Ub are recognized by a USP30-specific surface. Structure-based mutagenesis showed that the interface with the proximal Ub is critical for the specific cleavage of Lys6-linked Ub chains, together with the noncanonical catalytic triad composed of Cys-His-Ser. The structural findings presented here reveal a mechanism for Lys6-linkage-specific deubiquitination.Entities:
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Year: 2017 PMID： 28945247 DOI： 10.1038/nsmb.3469
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN： 1545-9985 Impact factor: 15.369