Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase

Tapan Biswas, Oleg V. Tsodikov

Research output: Contribution to journalArticlepeer-review

48 Scopus citations


Hexameric DnaB helicase unwinds the DNA double helix during replication of genetic material in bacteria. DnaB is an essential bacterial protein; therefore, it is an important potential target for antibacterial drug discovery. We report a crystal structure of the N-terminal region of DnaB from the pathogen Mycobacterium tuberculosis (MtDnaBn), determined at 2.0 Å resolution. This structure provides atomic resolution details of formation of the hexameric ring of DnaB by two distinct interfaces. An extensive hydrophobic interface stabilizes a dimer of MtDnaBn by forming a four-helix bundle. The other, less extensive, interface is formed between the dimers, connecting three of them into a hexameric ring. On the basis of crystal packing interactions between MtDnaBn rings, we suggest a model of a helicase-primase complex that explains previously observed effects of DnaB mutations on DNA priming.

Original languageEnglish
Pages (from-to)3064-3071
Number of pages8
JournalFEBS Journal
Issue number12
StatePublished - Jun 2008


  • Crystal structure
  • DnaB helicase
  • Primase
  • Replication
  • Tuberculosis

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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