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The recruitment of the hexameric DnaB helicase to the origin of replication is mediated by distinct mechanisms that rely on specialized factors known as helicase loaders. The DciA family of helicase loaders exhibits distinct architectures that differ in the arrangement of the KH and DnaB\u2010binding lasso domains. In this study, we probe the predicted structural architecture of the\n                    <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n                    (\n                    <jats:italic>Mt<\/jats:italic>\n                    ) DciA helicase loader and its interplay with the cognate helicase\n                    <jats:italic>Mt<\/jats:italic>\n                    DnaB. Native mass spectrometry and small\u2010angle X\u2010ray scattering (SAXS) analyses reveal that\n                    <jats:italic>Mt<\/jats:italic>\n                    DciA adopts a monomeric and compact architecture in solution. We demonstrate that\n                    <jats:italic>Mt<\/jats:italic>\n                    DnaB binds\n                    <jats:italic>Mt<\/jats:italic>\n                    DciA with nanomolar affinity, likely forming a 2:1 complex at the Docking Helix\u2013Linker Helix (DH\u2010LH) interface of the replicative helicase. We predict that the intein\u2010containing immature\n                    <jats:italic>Mt<\/jats:italic>\n                    DnaB\n                    <jats:sup>i<\/jats:sup>\n                    will fail to form the active hexamer. As such, we suggest that\n                    <jats:italic>Mt<\/jats:italic>\n                    DciA will show little to no affinity for intein\u2010containing\n                    <jats:italic>Mt<\/jats:italic>\n                    DnaB\n                    <jats:sup>i<\/jats:sup>\n                    .\n                  <\/jats:p>","DOI":"10.1002\/pro.70771","type":"journal-article","created":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T11:39:55Z","timestamp":1787571595000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Structural and biophysical characterization of\n                    <i>Mycobacterium tuberculosis<\/i>\n                    <scp>DciA<\/scp>\n                    reveals functional convergence in\n                    <scp>DnaB<\/scp>\n                    helicase recognition"],"prefix":"10.1002","volume":"35","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0711-8269","authenticated-orcid":false,"given":"Daniele","family":"Mazzoletti","sequence":"first","affiliation":[{"name":"Department of Pharmaceutical Sciences University of Piemonte Orientale  Novara Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-2567-7624","authenticated-orcid":false,"given":"Andrea","family":"Garavaglia","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences University of Piemonte Orientale  Novara Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0093-0921","authenticated-orcid":false,"given":"Hayden","family":"Fisher","sequence":"additional","affiliation":[{"name":"European Synchrotron Radiation Facility  Grenoble 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