Structural highlights
Function
[DNAB_MYCTU] Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity (By similarity). The intein is an endonuclease (Potential).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 A 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.
Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase.,Biswas T, Tsodikov OV FEBS J. 2008 Jun;275(12):3064-71. Epub 2008 May 8. PMID:18479467[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Biswas T, Tsodikov OV. Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase. FEBS J. 2008 Jun;275(12):3064-71. Epub 2008 May 8. PMID:18479467 doi:10.1111/j.1742-4658.2008.06460.x
