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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2021,1,12]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>\n                    Bacteria possess a sophisticated arsenal of defense mechanisms that allow them to survive in adverse conditions. Adaptation to acid stress and hypoxia is crucial for the enterobacterial transmission in the gastrointestinal tract of their human host. When subjected to low pH,\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    and many other enterobacteria activate a proton-consuming resistance system based on the acid stress-inducible lysine decarboxylase LdcI. Here we develop generally applicable tools to uncover the spatial localization of LdcI inside the cell by superresolution fluorescence microscopy and investigate the in vitro supramolecular organization of this enzyme by cryo-EM. We build on these results to propose a mechanistic model for LdcI function and offer tools for further in vivo investigations.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2014383118","type":"journal-article","created":{"date-parts":[[2020,12,28]],"date-time":"2020-12-28T16:33:26Z","timestamp":1609173206000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":17,"title":["Supramolecular assembly of the\n                    <i>Escherichia coli<\/i>\n                    LdcI upon acid stress"],"prefix":"10.1073","volume":"118","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8880-4481","authenticated-orcid":false,"given":"Matthew","family":"Jessop","sequence":"first","affiliation":[{"name":"Institut de Biologie Structurale (IBS), Universit\u00e9 Grenoble Alpes (UGA), Commissariat \u00e0 l'\u00e9nergie atomique et aux \u00e9nergies alternatives (CEA), CNRS, F-38044 Grenoble, 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