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== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/A0A085R2T8_VIBCL A0A085R2T8_VIBCL]] Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.[ARBA:ARBA00003574][RuleBase:RU362085]
[[https://www.uniprot.org/uniprot/A0A085R2T8_VIBCL A0A085R2T8_VIBCL]] Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.[ARBA:ARBA00003574][RuleBase:RU362085]
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== Publication Abstract from PubMed ==
To enable chromosomal replication, DNA is unwound by the ATPase molecular motor replicative helicase. The bacterial helicase DnaB is a ring-shaped homo-hexamer whose conformational dynamics are being studied through its different 3D structural states adopted along its functional cycle. Our findings describe a new crystal structure for the apo-DnaB from Vibrio cholerae, forming a planar hexamer with pseudo-symmetry, constituted by a trimer of dimers in which the C-terminal domains delimit a triskelion-shaped hole. This hexamer is labile and inactive. We suggest that it represents an intermediate state allowing the formation of the active NTP-bound hexamer from dimers.
The apo-form of the Vibrio cholerae replicative helicase DnaB is a labile and inactive planar trimer of dimers.,Cargemel C, Walbott H, Durand D, Legrand P, Ouldali M, Ferat JL, Marsin S, Quevillon-Cheruel S FEBS Lett. 2022 May 14. doi: 10.1002/1873-3468.14403. PMID:35568982<ref>PMID:35568982</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>

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