Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation.
about
Mechanisms for initiating cellular DNA replicationThe crystal structure of the Thermus aquaticus DnaB helicase monomerThe structure of a DnaB-family replicative helicase and its interactions with primaseHexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicaseCrystal Structure and Mode of Helicase Binding of the C-Terminal Domain of Primase from Helicobacter pyloriNucleotide and Partner-Protein Control of Bacterial Replicative Helicase Structure and FunctionPrimase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficileStructural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria.Two distantly homologous DnaG primases from Thermoanaerobacter tengcongensis exhibit distinct initiation specificities and priming activitiesRegulation of bacterial priming and daughter strand synthesis through helicase-primase interactionsA novel non-radioactive primase-pyrophosphatase activity assay and its application to the discovery of inhibitors of Mycobacterium tuberculosis primase DnaGDomain swapping reveals that the C- and N-terminal domains of DnaG and DnaB, respectively, are functional homologues.Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.The bacterial helicase-primase interaction: a common structural/functional module.Loading mechanisms of ring helicases at replication origins.Bacterial DNA replication enzymes as targets for antibacterial drug discovery.Functional interplay of DnaE polymerase, DnaG primase and DnaC helicase within a ternary complex, and primase to polymerase hand-off during lagging strand DNA replication in Bacillus subtilis.Class-specific restrictions define primase interactions with DNA template and replicative helicase.Conserved residues of the C-terminal p16 domain of primase are involved in modulating the activity of the bacterial primosome.Bacterial protein structures reveal phylum dependent divergence.In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues.DnaC, the indispensable companion of DnaB helicase, controls the accessibility of DnaB helicase by primase.The Macromolecular Machines that Duplicate the Escherichia coli Chromosome as Targets for Drug Discovery.¹H, ¹³C, and ¹⁵N NMR assignments for the helicase interaction domain of Staphylococcus aureus DnaG primase.Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori.DnaG Primase-A Target for the Development of Novel Antibacterial Agents
P2860
Q26827264-41787804-C09F-4567-933B-4713135730D8Q27646527-E243F5BC-D58C-4C0A-BB99-DE14E02C6DC2Q27649417-AE9EA0A8-2120-468C-BE24-9B4DC20CF611Q27650607-20350492-FE47-4FFC-9E67-F21FCDB6670FQ27677366-79995DE7-53C2-46F3-A9D9-BCFF8E9AF23BQ27681112-59B56F80-8209-49E7-8E68-9346974AE364Q28357054-CA9A53F3-B095-4637-8436-D2EA48E928CBQ33677529-42637A52-DC76-4AC0-B7A4-7C787B08C74DQ33876870-3E0C2D77-CEC3-4124-A590-9EA4157933DAQ33999043-AF800A65-84D4-4A9C-9C0E-A2B85A58E58DQ34319571-DEDAC847-F9D1-4A2F-8A31-BA363D61135BQ34558338-894CA7BD-780A-4A06-AD1C-E46A557A8FF2Q35791501-50CDF885-E377-4EFC-AC5B-304AD19966BEQ36153494-E874E556-7FD1-4299-AC93-0D47936D06BAQ37993607-E7CEE30F-B75D-4E5E-B4B8-E4D6369DFA1DQ37998090-9F3001CB-9ECF-40E2-B2C4-E3E27608C22AQ41074421-FB92C187-72AA-4D34-8A67-0A681E7BE696Q41433325-89EF31E3-A516-4668-A971-EB3BFA599F93Q41955522-DF8941B7-A342-4945-93F4-9EDA461DA08CQ42047721-DE992D62-37BB-4701-A438-91CE80CA108CQ43203582-2404318F-644D-4BCF-BD1B-A128F6210772Q47603277-A825D493-4CEA-47A7-9C67-8A1F3E92DE32Q52656083-C88C35ED-A58A-4936-831A-AC0CCC36E62CQ54584769-F4420332-141E-4B93-A6FD-9E9DBF1964EDQ55026915-91E5E087-C677-4E70-907A-9EC4398BDB3BQ58783987-1E01B4D6-1DDA-4145-86F6-C21ABF30AB81
P2860
Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Solution structure of the heli ...... model for helicase activation.
@en
type
label
Solution structure of the heli ...... model for helicase activation.
@en
prefLabel
Solution structure of the heli ...... model for helicase activation.
@en
P2093
P2860
P1433
P1476
Solution structure of the heli ...... model for helicase activation
@en
P2093
Andrea M Hounslow
Jenny Thirlway
Karl Syson
P2860
P304
P356
10.1016/J.STR.2005.01.022
P577
2005-04-01T00:00:00Z