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During the infection, Legionella injects more than 300 effector proteins into host cells. Among them are enzymes involved in altering the host-ubiquitination system. Here, we identified two\n                    <jats:bold>\n                      <jats:underline>L<\/jats:underline>\n                    <\/jats:bold>\n                    egionella\n                    <jats:bold>\n                      <jats:underline>OT<\/jats:underline>\n                    <\/jats:bold>\n                    U (ovarian tumor)-like deubiquitinases (LOT-DUBs; LotB [Lpg1621\/Ceg23] and LotC [Lpg2529]). The crystal structure of the LotC catalytic core (LotC\n                    <jats:sub>14-310<\/jats:sub>\n                    ) was determined at 2.4 \u212b. Unlike the classical OTU-family, the LOT-family shows an extended helical lobe between the Cys-loop and the variable loop, which defines them as a unique class of OTU-DUBs. LotB has an additional ubiquitin-binding site (S1\u2019), which enables the specific cleavage of Lys63-linked polyubiquitin chains. By contrast, LotC only contains the S1 site and cleaves different species of ubiquitin chains. MS analysis of LotB and LotC identified different categories of host-interacting proteins and substrates. Together, our results provide new structural insights into bacterial OTU-DUBs and indicate distinct roles in host\u2013pathogen interactions.\n                  <\/jats:p>","DOI":"10.7554\/elife.58277","type":"journal-article","created":{"date-parts":[[2020,11,13]],"date-time":"2020-11-13T08:00:20Z","timestamp":1605254420000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.58277","source":"Crossref","is-referenced-by-count":38,"title":["Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection"],"prefix":"10.7554","volume":"9","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8272-6133","authenticated-orcid":true,"given":"Donghyuk","family":"Shin","sequence":"first","affiliation":[{"name":"Institute of Biochemistry II, Faculty of Medicine, Goethe University Frankfurt, Frankfurt, Germany"},{"name":"Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt, Germany"},{"name":"Max Planck Institute of Biophysics, Frankfurt, Germany"},{"name":"Department of Nano-Bioengineering, Incheon National University, Incheon, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7383-3594","authenticated-orcid":true,"given":"Anshu","family":"Bhattacharya","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry II, Faculty of Medicine, Goethe University Frankfurt, Frankfurt, Germany"},{"name":"Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3603-5913","authenticated-orcid":true,"given":"Yi-Lin","family":"Cheng","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry II, Faculty of Medicine, Goethe University Frankfurt, Frankfurt, Germany"},{"name":"Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt, 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