{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,18]],"date-time":"2026-10-18T13:35:16Z","timestamp":1792330516148,"version":"4.4.0"},"reference-count":48,"publisher":"National Academy of Sciences","issue":"51","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2009,12,22]]},"abstract":"<jats:p>\n                    Iron deprivation activates the expression of components of the siderophore-mediated iron acquisition systems in\n                    <jats:italic>Bacillus subtilis<\/jats:italic>\n                    , including not only the synthesis and uptake of its siderophore bacillibactin but also expression of multiple ABC transporters for iron scavenging using xenosiderophores. The\n                    <jats:italic>yclNOPQ<\/jats:italic>\n                    operon is shown to encode the complete transporter for petrobactin (PB), a photoreactive 3,4-catecholate siderophore produced by many members of the\n                    <jats:italic>B. cereus<\/jats:italic>\n                    group, including\n                    <jats:italic>B. anthracis<\/jats:italic>\n                    . Isogenic disruption mutants in the\n                    <jats:italic>yclNOPQ<\/jats:italic>\n                    transporter, including permease YclN, ATPase YclP, and a substrate-binding protein YclQ, are unable to use either PB or the photoproduct of FePB (FePB\n                    <jats:sup>\u03bd<\/jats:sup>\n                    ) for iron delivery and growth, in contrast to the wild-type\n                    <jats:italic>B. subtilis<\/jats:italic>\n                    . Complementation of the mutations with the copies of the respective genes restores this capability. The YclQ receptor binds selectively iron-free and ferric PB, the PB precursor, 3,4-dihydroxybenzoic acid (3,4-DHB), and FePB\n                    <jats:sup>\u03bd<\/jats:sup>\n                    with high affinity; the ferric complexes are seen in ESI-MS, implying strong electrostatic interaction between the protein-binding pocket and siderophore. The first structure of a Gram-positive siderophore receptor is presented. The 1.75-\u212b crystal structure of YclQ reveals a bilobal periplasmic binding protein (PBP) fold consisting of two \u03b1\/\u03b2\/\u03b1 sandwich domains connected by a long \u03b1-helix with the binding pocket containing conserved positively charged and aromatic residues and large enough to accommodate FePB. Orthologs of the\n                    <jats:italic>B. subtilis<\/jats:italic>\n                    PB-transporter YclNOPQ in PB-producing\n                    <jats:italic>Bacilli<\/jats:italic>\n                    are likely contributors to the pathogenicity of these species and provide a potential target for antibacterial strategies.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0904793106","type":"journal-article","created":{"date-parts":[[2009,12,2]],"date-time":"2009-12-02T23:03:53Z","timestamp":1259795033000},"page":"21854-21859","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":96,"title":["Characterization of a\n                    <i>Bacillus subtilis<\/i>\n                    transporter for petrobactin, an anthrax stealth siderophore"],"prefix":"10.1073","volume":"106","author":[{"given":"Anna M.","family":"Zawadzka","sequence":"first","affiliation":[{"name":"Department of Chemistry, University of California, Berkeley, CA 94720-1460; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Youngchang","family":"Kim","sequence":"additional","affiliation":[{"name":"Biosciences Division, Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne, IL 60439"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalia","family":"Maltseva","sequence":"additional","affiliation":[{"name":"Biosciences Division, Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne, IL 60439"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rita","family":"Nichiporuk","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of California, Berkeley, CA 94720-1460; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yao","family":"Fan","sequence":"additional","affiliation":[{"name":"Biosciences Division, Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne, IL 60439"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrzej","family":"Joachimiak","sequence":"additional","affiliation":[{"name":"Biosciences Division, Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne, IL 60439"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kenneth N.","family":"Raymond","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of California, Berkeley, CA 94720-1460; and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2009,12,22]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0168-6445(03)00055-X"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.00012-07"},{"key":"e_1_3_3_3_2","first-page":"387","volume-title":"Iron Transport in Bacteria","author":"Heinrichs DE","year":"2004","unstructured":"DE Heinrichs, A Rahn, SE Dale, MT Sebulsky, Iron transport systems in pathogenic bacteria: Staphylococcus, Streptococcus, and Bacillus. 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