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2r5u

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Revision as of 06:14, 28 May 2008

Image:2r5u.jpg

Template:STRUCTURE 2r5u

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


Overview

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.

About this Structure

2R5U is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Wed May 28 09:14:29 2008

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