Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling (Q41791841)

10 October 2017

title

Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling (English)

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10 October 2017

James M Berger

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10 October 2017

Jan P Erzberger

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10 October 2017

Melissa L Mott

series ordinal

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10 October 2017

publication date

9 July 2006

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Nature Structural & Molecular Biology

10 October 2017

published in

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10 October 2017

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10 October 2017

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10 October 2017

page(s)

676-683

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Common domains in the initiators of DNA replication in Bacteria, Archaea and Eukarya: combined structural, functional and phylogenetic perspectives.

10 October 2017

cites work

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Evolutionary relationships and structural mechanisms of AAA+ proteins

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ATPase switches controlling DNA replication initiation.

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The DnaC helicase loader is a dual ATP/ADP switch protein

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Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli

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Structural basis of replication origin recognition by the DnaA protein

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Unraveling the early steps of prokaryotic replication

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Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex

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The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation

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Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains

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Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease

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Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein

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Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP

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The box VII motif of Escherichia coli DnaA protein is required for DnaA oligomerization at the E. coli replication origin

21 January 2018

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Formation of an ATP-DnaA-specific initiation complex requires DnaA Arginine 285, a conserved motif in the AAA+ protein family.

21 January 2018

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DNA replication-coupled inactivation of DnaA protein in vitro: a role for DnaA arginine-334 of the AAA+ Box VIII motif in ATP hydrolysis

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A model for initiation at origins of DNA replication

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Topological domain structure of the Escherichia coli chromosome

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The dnaA protein complex with the E. coli chromosomal replication origin (oriC) and other DNA sites.

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Mechanism of origin unwinding: sequential binding of DnaA to double- and single-stranded DNA

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Two discriminatory binding sites in the Escherichia coli replication origin are required for DNA strand opening by initiator DnaA-ATP.

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Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen

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Molecular mechanism of DNA replication-coupled inactivation of the initiator protein in Escherichia coli: interaction of DnaA with the sliding clamp-loaded DNA and the sliding clamp-Hda complex.

21 January 2018

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Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex

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Domains of DnaA protein involved in interaction with DnaB protein, and in unwinding the Escherichia coli chromosomal origin.

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Archaea: an archetype for replication initiation studies?

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DNA topology, not DNA sequence, is a critical determinant for Drosophila ORC-DNA binding

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Functions of sensor 1 and sensor 2 regions of Saccharomyces cerevisiae Cdc6p in vivo and in vitro

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Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicase

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A structural role for ATP in the formation and stability of the human origin recognition complex

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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

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Pushing the boundaries of molecular replacement with maximum likelihood

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Maximum-likelihood density modification

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

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ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information

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Replisome assembly at oriC, the replication origin of E. coli, reveals an explanation for initiation sites outside an origin

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Escherichia coli DnaA protein. The N-terminal domain and loading of DnaB helicase at the E. coli chromosomal origin

31 March 2020

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Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex.

31 March 2020

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Improving macromolecular electrostatics calculations

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSMB1115

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10 October 2017

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