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TitleStructural insights into ubiquitin chain cleavage by ovarian tumor deubiquitinases.
Journal, issue, pagesLife Sci Alliance, Vol. 6, Issue 7, Year 2023
Publish dateApr 26, 2023
AuthorsSangwoo Kang / Gyuhee Kim / Minhyeong Choi / Minwoo Jeong / Gerbrand J van der Heden van Noort / Soung-Hun Roh / Donghyuk Shin /
PubMed AbstractAlthough ubiquitin is found only in eukaryotes, several pathogenic bacteria and viruses possess proteins that hinder the host ubiquitin system. , a gram-negative intracellular bacterium, possesses an ...Although ubiquitin is found only in eukaryotes, several pathogenic bacteria and viruses possess proteins that hinder the host ubiquitin system. , a gram-negative intracellular bacterium, possesses an ovarian tumor (OTU) family of deubiquitinases (Lot DUBs). Herein, we describe the molecular characteristics of Lot DUBs. We elucidated the structure of the LotA OTU1 domain and revealed that entire Lot DUBs possess a characteristic extended helical lobe that is not found in other OTU-DUBs. The structural topology of an extended helical lobe is the same throughout the Lot family, and it provides an S1' ubiquitin-binding site. Moreover, the catalytic triads of Lot DUBs resemble those of the A20-type OTU-DUBs. Furthermore, we revealed a unique mechanism by which LotA OTU domains cooperate together to distinguish the length of the chain and preferentially cleave longer K48-linked polyubiquitin chains. The LotA OTU1 domain itself cleaves K6-linked ubiquitin chains, whereas it is also essential for assisting the cleavage of longer K48-linked polyubiquitin chains by the OTU2 domain. Thus, this study provides novel insights into the structure and mechanism of action of Lot DUBs.
External linksLife Sci Alliance / PubMed:37100438 / PubMed Central
MethodsEM (single particle)
Resolution15.0 Å
Structure data

EMDB-34350: Legionella pneumophila Deubiquitinase, LotA(7-544) apo state
Method: EM (single particle) / Resolution: 15.0 Å

Source
  • Legionella pneumophila (bacteria)

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