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Publication Abstract from PubMed

To better understand the poor conservation of helicase binding domain of primases/DnaG's among the eubacteria, we have determined the crystal structure of the Helicobacter pylori DnaG-CTD at 1.78 A. The structure has a globular subdomain connected to a helical hairpin. Structural comparison has revealed that globular subdomains despite the variation in number of helices have broadly similar arrangements across the species, whereas helical hairpins show different orientations. Further, to study the helicase-primase interaction in H. pylori (Hp), a complex was modeled using the HpDnaG-CTD and HpDnaB-NTD (helicase) crystal structures with the Bacillus stearothermophilus BstDnaB-BstDnaG-CTD (helicase-primase) complex structure as a template. Through the model a non-conserved critical residue Phe534 on helicase binding interface of DnaG-CTD was identified. Mutation guided by molecular dynamics, biophysical and biochemical studies validated our model. We have further concluded that species specific helicase-primase interactions are influenced by electrostatic surface potentials apart from the critical hydrophobic surface residues.

Crystal structure and mode of helicase binding of the C-terminal domain of primase from Helicobacter pylori.,Abdul Rehman SA, Verma V, Mazumder M, Dhar SK, Gourinath S J Bacteriol. 2013 Apr 12. PMID:23585534^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.