2R5U

Crystal structure of the N-terminal domain of DnaB helicase from Mycobacterium tuberculosis

Summary for 2R5U

• Entry DOI: 10.2210/pdb2r5u/pdb
• Descriptor: Replicative DNA helicase, GLYCEROL (3 entities in total)
• Functional Keywords: dnab, helicase, primase, replication, atp-binding, autocatalytic cleavage, dna replication, dna-binding, endonuclease, hydrolase, intron homing, nuclease, nucleotide-binding, primosome
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 6
• Total formula weight: 128334.90

Authors

Biswas, T.,Tsodikov, O.V. (deposition date: 2007-09-04, release date: 2008-05-27, Last modification date: 2024-02-21)

Primary citation

Biswas, T.,Tsodikov, O.V.
Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase.
Febs J., 275:3064-3071, 2008

PubMed Abstract: 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.

PubMed: 18479467
DOI: 10.1111/j.1742-4658.2008.06460.x

Experimental method

X-RAY DIFFRACTION (1.9 Å)