Structural basis of substrate recognition by a bacterial deubiquitinase important for dynamics of phagosome ubiquitination
Proceedings of the National Academy of Sciences of the United States of America, ISSN: 1091-6490, Vol: 112, Issue: 49, Page: 15090-15095
2015
- 86Citations
- 69Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations86
- Citation Indexes85
- 85
- CrossRef69
- Patent Family Citations1
- Patent Families1
- Captures69
- Readers69
- 69
Article Description
Manipulation of the host's ubiquitin network is emerging as an important strategy for counteracting and repurposing the posttranslational modification machineries of the host by pathogens. Ubiquitin E3 ligases encoded by infectious agents are well known, as are a variety of viral deubiquitinases (DUBs). Bacterial DUBs have been discovered, but little is known about the structure and mechanism underlying their ubiquitin recognition. In this report, we found that members of the Legionella pneumophila SidE effector family harbor a DUB module important for ubiquitin dynamics on the bacterial phagosome. Structural analysis of this domain alone and in complex with ubiquitin vinyl methyl ester (Ub-VME) reveals unique molecular contacts used in ubiquitin recognition. Instead of relying on the Ile44 patch of ubiquitin, as commonly used in eukaryotic counterparts, the SdeA module engages Gln40 of ubiquitin. The architecture of the active-site cleft presents an open arrangement with conformational plasticity, permitting deubiquitination of three of the most abundant polyubiquitin chains, with a distinct preference for Lys63 linkages. We have shown that this preference enables efficient removal of Lys63 linkages from the phagosomal surface. Remarkably, the structure reveals by far the most parsimonious use of molecular contacts to achieve deubiquitination, with less than 1,000 of accessible surface area buried upon complex formation with ubiquitin. This type of molecular recognition appears to enable dual specificity toward ubiquitin and the ubiquitin-like modifier NEDD8.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84949197700&origin=inward; http://dx.doi.org/10.1073/pnas.1514568112; http://www.ncbi.nlm.nih.gov/pubmed/26598703; https://pnas.org/doi/full/10.1073/pnas.1514568112; https://dx.doi.org/10.1073/pnas.1514568112; https://www.pnas.org/content/112/49/15090
Proceedings of the National Academy of Sciences
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