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The structure of a DnaB-family replicative helicase and its interactions with primase

The structure of a DnaB-family replicative helicase and its interactions with primase

http://www.wikidata.org/entity/Q27649417

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Replisome Assembly at Bacterial Chromosomes and Iteron Plasmids Structural Mechanisms of Hexameric Helicase Loading, Assembly, and Unwinding Mechanisms for initiating cellular DNA replication Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase Structure and primase-mediated activation of a bacterial dodecameric replicative helicase Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader Three-Dimensional Structure of N-Terminal Domain of DnaB Helicase and Helicase-Primase Interactions in Helicobacter pylori The hexameric helicase DnaB adopts a nonplanar conformation during translocation.Nucleotide and Partner-Protein Control of Bacterial Replicative Helicase Structure and Function Structural Basis for the Interaction of a Hexameric Replicative Helicase with the Regulatory Subunit of Human DNA Polymerase -Primase Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile DNA binding activity of Helicobacter pylori DnaB helicase: the role of the N-terminal domain in modulating DNA binding activities Biochemical Characterization of a Mycobacteriophage Derived DnaB Ortholog Reveals New Insight into the Evolutionary Origin of DnaB Helicases Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes Residues in the central beta-hairpin of the DNA helicase of bacteriophage T7 are important in DNA unwinding.A specific docking site for DNA polymerase {alpha}-primase on the SV40 helicase is required for viral primosome activity, but helicase activity is dispensable Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases.The mini-chromosome maintenance (Mcm) complexes interact with DNA polymerase α-primase and stimulate its ability to synthesize RNA primers DnaC traps DnaB as an open ring and remodels the domain that binds primase.Bacteriophage SPP1 DNA replication strategies promote viral and disable host replication in vitro.Physiological and biochemical defects in carboxyl-terminal mutants of mitochondrial DNA helicase.The bacterial DnaC helicase loader is a DnaB ring breaker.On helicases and other motor proteins.A biochemically active MCM-like helicase in Bacillus cereus The Mcm complex: unwinding the mechanism of a replicative helicase.Single-molecule fluorescence reveals the unwinding stepping mechanism of replicative helicase.Origin DNA melting and unwinding in DNA replication.Bacterial DNA replication enzymes as targets for antibacterial drug discovery.Loading strategies of ring-shaped nucleic acid translocases and helicases.cryo-EM structures of the E. coli replicative DNA polymerase reveal its dynamic interactions with the DNA sliding clamp, exonuclease and τ.Genomics Analysis of Replicative Helicase DnaB Sequences in Proteobacteria DnaC, the indispensable companion of DnaB helicase, controls the accessibility of DnaB helicase by primase.Bacterial DnaB helicase interacts with the excluded strand to regulate unwinding.

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The structure of a DnaB-family replicative helicase and its interactions with primase

http://www.wikidata.org/entity/Q27649417

description

2008 nî lūn-bûn

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2008 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

The structure of a DnaB-family replicative helicase and its interactions with primase

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The structure of a DnaB-family replicative helicase and its interactions with primase

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The structure of a DnaB-family replicative helicase and its interactions with primase

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The structure of a DnaB-family replicative helicase and its interactions with primase

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The structure of a DnaB-family replicative helicase and its interactions with primase

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The structure of a DnaB-family replicative helicase and its interactions with primase

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The structure of a DnaB-family replicative helicase and its interactions with primase

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The structure of a DnaB-family replicative helicase and its interactions with primase

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The structure of a DnaB-family replicative helicase and its interactions with primase

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The structure of a DnaB-family replicative helicase and its interactions with primase

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Etienne Tokonzaba

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Ganggang Wang

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Michael G Klein

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Xiaojiang S Chen

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Yi Zhang

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P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer

Crystal structure of the N-terminal domain of the DnaB hexameric helicase

Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7

Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides

Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase

Refinement of macromolecular structures by the maximum-likelihood method

Automated MAD and MIR structure solution

MOLREP: an Automated Program for Molecular Replacement

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1

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15

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18157148

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