Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation.

scientific article

Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/J.STR.2005.01.022
P932PMC publication ID3033578
P698PubMed publication ID15837199
P5875ResearchGate publication ID7900392

P50authorPanos SoultanasQ38317689
Jonathan WalthoQ63386282
Andrea M HounslowQ114740153
P2093author name stringKarl Syson
Jenny Thirlway
P2860cites workCrystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationQ26778405
NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamerQ27619049
Crystal structure of the N-terminal domain of the DnaB hexameric helicaseQ27619052
Structure of the RNA polymerase domain of E. coli primaseQ27621970
Structure of the zinc-binding domain of Bacillus stearothermophilus DNA primaseQ27622019
Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperonesQ27633681
AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMRQ27860778
Protein structure comparison by alignment of distance matricesQ27860798
Protein backbone angle restraints from searching a database for chemical shift and sequence homologyQ27861108
Flexibility of the rings: structural asymmetry in the DnaB hexameric helicaseQ30309878
DNA primasesQ33950235
Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA.Q36685433
Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication forkQ38311133
DnaB helicase stimulates primer synthesis activity on short oligonucleotide templatesQ38316011
The interaction between helicase and primase sets the replication fork clockQ38353757
The extreme C terminus of primase is required for interaction with DnaB at the replication forkQ38353761
Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus.Q38642649
DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric ringsQ40969310
The clamp-loader-helicase interaction in Bacillus. Atomic force microscopy reveals the structural organisation of the DnaB-tau complex in BacillusQ42105879
Effects of domain dissection on the folding and stability of the 43 kDa protein PGK probed by NMR.Q44512611
Expression, purification, crystallization, and NMR studies of the helicase interaction domain of Escherichia coli DnaG primase.Q51724788
ProDom: automated clustering of homologous domainsQ57935149
DnaB helicase affects the initiation specificity of Escherichia coli primase on single-stranded DNA templatesQ73394974
Trading places on DNA--a three-point switch underlies primer handoff from primase to the replicative DNA polymeraseQ78170535
Initiation of bidirectional replication at the chromosomal origin is directed by the interaction between helicase and primaseQ78239977
P433issue4
P921main subjectsolution structureQ99235426
P304page(s)609-616
P577publication date2005-04-01
P1433published inStructureQ15709970
P1476titleSolution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation
P478volume13

Reverse relations

cites work (P2860)
Q34319571A novel non-radioactive primase-pyrophosphatase activity assay and its application to the discovery of inhibitors of Mycobacterium tuberculosis primase DnaG
Q35791501Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target
Q37998090Bacterial DNA replication enzymes as targets for antibacterial drug discovery
Q42047721Bacterial protein structures reveal phylum dependent divergence
Q41433325Class-specific restrictions define primase interactions with DNA template and replicative helicase
Q41955522Conserved residues of the C-terminal p16 domain of primase are involved in modulating the activity of the bacterial primosome.
Q27677366Crystal Structure and Mode of Helicase Binding of the C-Terminal Domain of Primase from Helicobacter pylori
Q47603277DnaC, the indispensable companion of DnaB helicase, controls the accessibility of DnaB helicase by primase
Q58783987DnaG Primase-A Target for the Development of Novel Antibacterial Agents
Q34558338Domain swapping reveals that the C- and N-terminal domains of DnaG and DnaB, respectively, are functional homologues
Q41074421Functional 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
Q27650607Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase
Q46427393Identification of a Ligand-Binding Site on the Staphylococcus aureus DnaG Primase C-Terminal Domain.
Q43203582In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues
Q37993607Loading mechanisms of ring helicases at replication origins.
Q26827264Mechanisms for initiating cellular DNA replication
Q27681112Nucleotide and Partner-Protein Control of Bacterial Replicative Helicase Structure and Function
Q28357054Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile
Q33999043Regulation of bacterial priming and daughter strand synthesis through helicase-primase interactions
Q55026915Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori.
Q33677529Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria.
Q52656083The Macromolecular Machines that Duplicate the Escherichia coli Chromosome as Targets for Drug Discovery.
Q36153494The bacterial helicase-primase interaction: a common structural/functional module.
Q27646527The crystal structure of the Thermus aquaticus DnaB helicase monomer
Q27649417The structure of a DnaB-family replicative helicase and its interactions with primase
Q33876870Two distantly homologous DnaG primases from Thermoanaerobacter tengcongensis exhibit distinct initiation specificities and priming activities
Q54584769¹H, ¹³C, and ¹⁵N NMR assignments for the helicase interaction domain of Staphylococcus aureus DnaG primase.