PUBLICATION

Structural basis for specific cleavage of Lys6-linked polyubiquitin chains by USP30

Authors
Sato, Y., Okatsu, K., Saeki, Y., Yamano, K., Matsuda, N., Kaiho, A., Yamagata, A., Goto-Ito, S., Ishikawa, M., Hashimoto, Y., Tanaka, K., Fukai, S.
ID
ZDB-PUB-170926-3
Date
2017
Source
Nature structural & molecular biology   24(11): 911-919 (Journal)
Registered Authors
Keywords
none
MeSH Terms
  • Animals
  • Crystallography, X-Ray
  • DNA Mutational Analysis
  • Models, Molecular
  • Mutagenesis
  • Polyubiquitin/metabolism*
  • Protein Conformation
  • Ubiquitin-Specific Proteases/chemistry*
  • Ubiquitin-Specific Proteases/genetics
  • Ubiquitin-Specific Proteases/metabolism*
  • Zebrafish
PubMed
28945247 Full text @ Nat. Struct. Mol. Biol.
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.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping