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We show that\n                    <jats:styled-content style=\"fixed-case\">AtxA<\/jats:styled-content>\n                    crystallizes as a dimer. Distinct folds associated with predicted\n                    <jats:styled-content style=\"fixed-case\">DNA<\/jats:styled-content>\n                    \u2010binding domains (\n                    <jats:styled-content style=\"fixed-case\">HTH<\/jats:styled-content>\n                    1 and\n                    <jats:styled-content style=\"fixed-case\">HTH<\/jats:styled-content>\n                    2) and phosphoenolpyruvate: carbohydrate phosphotransferase system\u2010regulated domains (\n                    <jats:styled-content style=\"fixed-case\">PRD<\/jats:styled-content>\n                    1 and\n                    <jats:styled-content style=\"fixed-case\">PRD<\/jats:styled-content>\n                    2) are apparent. We tested\n                    <jats:styled-content style=\"fixed-case\">AtxA<\/jats:styled-content>\n                    variants containing single and double phosphomimetic (\n                    <jats:styled-content style=\"fixed-case\">H<\/jats:styled-content>\n                    is\u2192\n                    <jats:styled-content style=\"fixed-case\">A<\/jats:styled-content>\n                    sp) and phosphoablative (\n                    <jats:styled-content style=\"fixed-case\">H<\/jats:styled-content>\n                    is\u2192\n                    <jats:styled-content style=\"fixed-case\">A<\/jats:styled-content>\n                    la) amino acid changes for activity in\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>B<\/jats:italic>\n                    <\/jats:styled-content>\n                    <jats:italic>.\u2009anthracis<\/jats:italic>\n                    cultures and for protein\u2013protein interactions in cell lysates. Reduced activity of\n                    <jats:styled-content style=\"fixed-case\">AtxA<\/jats:styled-content>\n                    H199A, lack of multimerization and activity of\n                    <jats:styled-content style=\"fixed-case\">AtxA<\/jats:styled-content>\n                    H379D variants, and predicted structural changes associated with phosphorylation support a model for control of\n                    <jats:styled-content style=\"fixed-case\">AtxA<\/jats:styled-content>\n                    function. We propose that (i) in the\n                    <jats:styled-content style=\"fixed-case\">AtxA<\/jats:styled-content>\n                    dimer, phosphorylation of\n                    <jats:styled-content style=\"fixed-case\">H<\/jats:styled-content>\n                    199 in\n                    <jats:styled-content style=\"fixed-case\">PRD<\/jats:styled-content>\n                    1 affects\n                    <jats:styled-content style=\"fixed-case\">HTH<\/jats:styled-content>\n                    2 positioning, influencing\n                    <jats:styled-content style=\"fixed-case\">DNA<\/jats:styled-content>\n                    \u2010binding; and (ii) phosphorylation of\n                    <jats:styled-content style=\"fixed-case\">H<\/jats:styled-content>\n                    379 in\n                    <jats:styled-content style=\"fixed-case\">PRD<\/jats:styled-content>\n                    2 disrupts dimer formation. The\n                    <jats:styled-content style=\"fixed-case\">AtxA<\/jats:styled-content>\n                    structure is the first reported high\u2010resolution full\u2010length structure of a\n                    <jats:styled-content style=\"fixed-case\">PRD<\/jats:styled-content>\n                    \u2010containing regulator, and can serve as a model for proteins of this family, especially those that link virulence to bacterial metabolism.\n                  <\/jats:p>","DOI":"10.1111\/mmi.12867","type":"journal-article","created":{"date-parts":[[2014,11,17]],"date-time":"2014-11-17T08:51:55Z","timestamp":1416214315000},"page":"426-441","source":"Crossref","is-referenced-by-count":40,"title":["Crystal structure of\n                    <scp>\n                      <i>B<\/i>\n                    <\/scp>\n                    <i>acillus anthracis<\/i>\n                    virulence regulator\n                    <scp>AtxA<\/scp>\n                    and effects of phosphorylated histidines on multimerization and activity"],"prefix":"10.1111","volume":"95","author":[{"given":"Troy G.","family":"Hammerstrom","sequence":"first","affiliation":[{"name":"Department of Microbiology and Molecular Genetics The University of Texas Health Science Center at Houston  Houston TX USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lori B.","family":"Horton","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Molecular Genetics The University of Texas Health Science Center at Houston  Houston TX USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michelle C.","family":"Swick","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Molecular Genetics The University of Texas Health Science Center at Houston  Houston TX USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrzej","family":"Joachimiak","sequence":"additional","affiliation":[{"name":"Center for 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