Apr 22, 2016 · In the 19 Å resolution EM map, the undistorted and unopened helicase ring holds a robust loader density above the C-terminal RecA-like domain. Meanwhile, the path of the central DNA binding channel appears to be obstructed by the reconstructed loader density, implying its potential role as a checkpoint conformation to prevent the loading of immature complex onto DNA.
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Request PDF | On Mar 1, 2016, Yen-Chen Lin and others published EM structure of a helicase-loader complex depicting a 6:2 binding sub-stoichiometry from Geobacillus kaustophilus HTA426 | Find
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Loading the bacterial replicative helicase DnaB onto DNA requires a specific loader protein, DnaC/DnaI, which creates the loading-competent state by opening the DnaB hexameric ring. To understand the molecular mechanism by which DnaC/DnaI opens the DnaB ring, we solved 3.1-Å co-crystal structure of the interaction domains of Escherichia coli DnaB-DnaC.
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Apr 22, 2016 · OSTI.GOV Journal Article: EM structure of a helicase-loader complex depicting a 6:2 binding sub-stoichiometry from Geobacillus kaustophilus HTA426
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Background:Replication requires coordinated interactions among proteins/DNA.
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Jan 01, 2013 · Structure determination. The complex of BstDnaB helicase, BsuDnaI loader and the HBD of BstDnaG primase was obtained by first purifying the DnaB–DnaI complex using gel filtration chromatography and then adding the HBD of DnaG (Fig. 1).This procedure is the same as previously reported15.Analysis of the proteins in these crystals using mass spectrometry and tryptic digestion …
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Structure viewers. Molecule: EM map: Font size: [English] menu
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structure of the B570-kDa prepriming complex between the Bacillus subtilis loader protein and the Bacillus stearothermophilus helicase, as well as the helicase-binding domain of primase with a
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Mar 15, 2012 · Bin Liu, William K. Eliason and Thomas A. Steitz, Structure of a helicase–helicase loader complex reveals insights into the mechanism of bacterial primosome assembly, Nature Communications, 10.1038/ncomms3495, 4, (2013).
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Hexameric DnaB helicases are often loaded at DNA replication forks by interacting with the initiator protein DnaA and/or a helicase loader (DnaC in Escherichia coli). These loaders are not universally required, and DnaB from Helicobacter pylori was found to bypass DnaC when expressed in E. coli cells. The crystal structure of Helicobacter pylori DnaB C-terminal domain (HpDnaB-CTD) reveals a
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Dec 01, 2012 · Structure determination. The complex of BstDnaB helicase, BsuDnaI loader and the HBD of BstDnaG primase was obtained by first purifying the DnaB–DnaI complex using gel filtration chromatography and then adding the HBD of DnaG (Fig. 1).This procedure is the same as previously reported15.Analysis of the proteins in these crystals using mass spectrometry and tryptic digestion …
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Hexameric DnaB helicases are often loaded at DNA replication forks by interacting with the initiator protein DnaA and/or a helicase loader (DnaC in Escherichia coli). These loaders are not universally required, and DnaB from Helicobacter pylori was found to bypass DnaC when expressed in E. coli cells. The crystal structure of Helicobacter pylori DnaB C-terminal domain (HpDnaB-CTD) reveals a
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2. CMG Helicase Is a Central Scaffold for Replisome Organization Replicative helicases act in the context of a large machinery re-ferredtoasthe "replisome."Repli-somes contain, at a minimum, a helicase, primase, DNA polymer-ases, sliding clamps, and a clamp loader in all cell types (reviewed in Refs. [1,2,14,29,35,36]). While the
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Bacillus stearothermophilus the helicase–primase interac-tion may not be transient, as was shown to be the case in E. coli (11). In Gram-positive bacteria, such as Bacillus subtilis, the replicative hexameric helicase is named DnaC (12). Notably, DnaC in E. coli is a helicase loader protein rather than a helicase. DnaC and DnaG from B. subtilis
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Request PDF | Crystal structure of the complex of the interaction domains of E. coli DnaB helicase and DnaC helicase loader: Structural basis implying a distortion-accumulation mechanism for the
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Sep 19, 2013 · Structure of a helicase–helicase loader complex reveals insights into the mechanism of bacterial primosome assembly Structure of a helicase–helicase loader complex reveals insights into the mechanism of bacterial primosome assembly. Access Restriction Open. Author: Liu, Bin ♦ Eliason, William K. ♦ Steitz, Thomas A.
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Sep 19, 2013 · During the assembly of the bacterial loader-dependent primosome, helicase loader proteins bind to the hexameric helicase ring, deliver it onto the oriC …
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Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly. Liu B., Eliason W.K., Steitz T.A. During the assembly of the bacterial loader-dependent primosome, helicase loader proteins bind to the hexameric helicase ring, deliver it onto the oriC DNA and then dissociate from the complex.
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The overall architecture of the complex exhibits a three-layered ring conformation. Moreover, the structure combined with the proposed model suggests that the shift from the 'open-ring' to the 'open-spiral' and then the 'closed-spiral' state of the helicase ring due to the binding of single-stranded DNA may be the cause of the loader release.
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Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly Bin Liu, William K. Eliason, Thomas A. Steitz Hormel Institute
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