{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T06:17:53Z","timestamp":1791267473253,"version":"4.1.0"},"reference-count":42,"publisher":"National Academy of Sciences","issue":"34","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2012,8,21]]},"abstract":"<jats:p>\n                    <jats:italic>Legionella pneumophila<\/jats:italic>\n                    is an opportunistic intracellular pathogen that causes sporadic and epidemic cases of Legionnaires\u2019 disease. Emerging data suggest that\n                    <jats:italic>Legionella<\/jats:italic>\n                    infection involves the subversion of host phosphoinositide (PI) metabolism. However, how this bacterium actively manipulates PI lipids to benefit its infection is still an enigma. Here, we report that the\n                    <jats:italic>L. pneumophila<\/jats:italic>\n                    virulence factor SidF is a phosphatidylinositol polyphosphate 3-phosphatase that specifically hydrolyzes the D3 phosphate of PI(3,4)P\n                    <jats:sub>2<\/jats:sub>\n                    and PI(3,4,5)P\n                    <jats:sub>3<\/jats:sub>\n                    . This activity is necessary for anchoring of PI(4)P-binding effectors to bacterial phagosomes. Crystal structures of SidF and its complex with its substrate PI(3,4)P\n                    <jats:sub>2<\/jats:sub>\n                    reveal striking conformational rearrangement of residues at the catalytic site to form a cationic pocket that specifically accommodates the D4 phosphate group of the substrate. Thus, our findings unveil a unique\n                    <jats:italic>Legionella<\/jats:italic>\n                    PI phosphatase essential for the establishment of lipid identity of bacterial phagosomes.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1207903109","type":"journal-article","created":{"date-parts":[[2012,8,8]],"date-time":"2012-08-08T01:22:10Z","timestamp":1344388930000},"page":"13567-13572","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":124,"title":["Structural basis for substrate recognition by a unique\n                    <i>Legionella<\/i>\n                    phosphoinositide phosphatase"],"prefix":"10.1073","volume":"109","author":[{"given":"FoSheng","family":"Hsu","sequence":"first","affiliation":[{"name":"Weill Institute for Cell and Molecular Biology,"},{"name":"Department of Molecular Biology and Genetics,"},{"name":"Graduate Field of Biochemistry, Molecular and Cell biology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wenhan","family":"Zhu","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lucy","family":"Brennan","sequence":"additional","affiliation":[{"name":"Graduate Field of Biophysics, Cornell University, Ithaca, NY 14853; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lili","family":"Tao","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhao-Qing","family":"Luo","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuxin","family":"Mao","sequence":"additional","affiliation":[{"name":"Weill Institute for Cell and Molecular Biology,"},{"name":"Department of Molecular Biology and Genetics,"},{"name":"Graduate Field of Biochemistry, Molecular and Cell biology, and"},{"name":"Graduate Field of Biophysics, Cornell University, Ithaca, NY 14853; and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2012,8,7]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1056\/NEJM197712012972202","article-title":"Legionnaires\u2019 disease: Isolation of a bacterium and demonstration of its role in other respiratory disease","volume":"297","author":"McDade JE","year":"1977","unstructured":"JE McDade, et al., Legionnaires\u2019 disease: Isolation of a bacterium and demonstration of its role in other respiratory disease. 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