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In the current study, our structural analysis of <jats:styled-content style=\"fixed-case\">BB<\/jats:styled-content>0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the <jats:styled-content style=\"fixed-case\">NADH<\/jats:styled-content>:quinone and ferredoxin:<jats:styled-content style=\"fixed-case\">NAD<\/jats:styled-content><jats:sup>+<\/jats:sup> sodium\u2010translocating oxidoreductase complexes, which points to a potential role for <jats:styled-content style=\"fixed-case\">BB<\/jats:styled-content>0365 as a component of the sodium pump. Additionally, <jats:styled-content style=\"fixed-case\">BB<\/jats:styled-content>0365 coordinated Zn<jats:sup>2+<\/jats:sup> by the His51, His55, His140 residues, and the Zn<jats:sup>2+<\/jats:sup>\u2010binding site indicates that <jats:styled-content style=\"fixed-case\">BB<\/jats:styled-content>0365 could act as a potential metalloenzyme; therefore, this structure narrows down the potential functions of <jats:styled-content style=\"fixed-case\">BB<\/jats:styled-content>0365, an essential protein for <jats:italic>B.\u00a0burgdorferi<\/jats:italic> to cause Lyme disease.<\/jats:p>","DOI":"10.1002\/1873-3468.13594","type":"journal-article","created":{"date-parts":[[2019,9,5]],"date-time":"2019-09-05T10:04:44Z","timestamp":1567677884000},"page":"317-326","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Structural analysis of <i>Borrelia\u00a0burgdorferi<\/i> periplasmic lipoprotein <scp>BB<\/scp>0365 involved in Lyme 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