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Most organisms, including\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Leptospira<\/jats:named-content>\n            , require divalent cations for proper growth, but because of their high reactivity, these metals are toxic at high concentrations. Therefore, bacteria have acquired strategies to maintain metal homeostasis, such as metal import and efflux. By screening\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Leptospira biflexa<\/jats:named-content>\n            transposon mutants for their ability to use Mn\n            <jats:sup>2+<\/jats:sup>\n            , we have identified a gene encoding a putative orphan ATP-binding cassette (ABC) ATPase of unknown function. Inactivation of this gene in both\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">L. biflexa<\/jats:named-content>\n            and\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">L. interrogans<\/jats:named-content>\n            strains led to mutants unable to grow in medium in which iron was replaced by Mn\n            <jats:sup>2+<\/jats:sup>\n            , suggesting an involvement of this ABC ATPase in divalent cation uptake. A mutation in this ATPase-coding gene increased susceptibility to Mn\n            <jats:sup>2+<\/jats:sup>\n            toxicity. Recombinant ABC ATPase of the pathogen\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">L. interrogans<\/jats:named-content>\n            exhibited Mg\n            <jats:sup>2+<\/jats:sup>\n            -dependent ATPase activity involving a P-loop motif. The structure of this ATPase was solved from a crystal containing two monomers in the asymmetric unit. Each monomer adopted a canonical two-subdomain organization of the ABC ATPase fold with an \u03b1\/\u03b2 subdomain containing the Walker motifs and an \u03b1 subdomain containing the ABC signature motif (LSSGE). The two monomers were arranged in a head-to-tail orientation, forming a V-shaped particle with all the conserved ABC motifs at the dimer interface, similar to functional ABC ATPases. These results provide the first structural and functional characterization of a leptospiral ABC ATPase.\n          <\/jats:p>","DOI":"10.1128\/jb.00915-13","type":"journal-article","created":{"date-parts":[[2013,10,12]],"date-time":"2013-10-12T01:21:53Z","timestamp":1381540913000},"page":"5583-5591","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":4,"title":["Structural and Functional Characterization of an Orphan ATP-Binding Cassette ATPase Involved in Manganese Utilization and Tolerance in Leptospira spp"],"prefix":"10.1128","volume":"195","author":[{"given":"Nadia","family":"Benaroudj","sequence":"first","affiliation":[{"name":"Institut Pasteur, Unit\u00e9 Biologie des Spiroch\u00e8tes, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frederick","family":"Saul","sequence":"additional","affiliation":[{"name":"Plate-Forme de Cristallographie, CNRS-UMR3528, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jacques","family":"Bellalou","sequence":"additional","affiliation":[{"name":"Plate-Forme Production de Prot\u00e9ines Recombinantes, CNRS-UMR3528, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabelle","family":"Miras","sequence":"additional","affiliation":[{"name":"Plate-Forme de Cristallographie, CNRS-UMR3528, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick","family":"Weber","sequence":"additional","affiliation":[{"name":"Plate-Forme de Cristallographie, CNRS-UMR3528, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincent","family":"Bondet","sequence":"additional","affiliation":[{"name":"Plate-Forme Production de Prot\u00e9ines Recombinantes, CNRS-UMR3528, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gerald L.","family":"Murray","sequence":"additional","affiliation":[{"name":"Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Department of Microbiology, Monash University, Clayton, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ben","family":"Adler","sequence":"additional","affiliation":[{"name":"Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Department of Microbiology, Monash University, Clayton, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paula","family":"Ristow","sequence":"additional","affiliation":[{"name":"Institut Pasteur, Unit\u00e9 Biologie des Spiroch\u00e8tes, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"H\u00e9l\u00e8ne","family":"Louvel","sequence":"additional","affiliation":[{"name":"Institut Pasteur, Unit\u00e9 Biologie des Spiroch\u00e8tes, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ahmed","family":"Haouz","sequence":"additional","affiliation":[{"name":"Plate-Forme de Cristallographie, CNRS-UMR3528, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mathieu","family":"Picardeau","sequence":"additional","affiliation":[{"name":"Institut Pasteur, Unit\u00e9 Biologie des Spiroch\u00e8tes, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1007\/s00775-008-0404-5","article-title":"Metal ions in biological catalysis: from enzyme databases to general principles","volume":"13","author":"Andreini C","year":"2008","unstructured":"AndreiniCBertiniICavallaroGHollidayGLThorntonJM. 2008. 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