4ehs

Crystal structure of Helicobacter pylori DnaG Primase C terminal domain

spinqualitylabelsall models 4ehs, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ehs is a 2 chain structure with sequence from Campylobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BME NonStd Res: MSE Gene: dnaG, DnaG Primase, HP_0012 (Campylobacter pylori) Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also RNA polymerase

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