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The internal workings of a DNA polymerase clamp-loading
Feb 01, 1999 · Hingorani MM, O'Donnell M. ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme. J Biol Chem. 1998 Sep 18; 273 (38):24550–24563. [Google Scholar] Kelman Z, O'Donnell M. DNA polymerase III holoenzyme: structure and function of a chromosomal replicating machine.
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Michael E. O'Donnell - Publications
ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme. The Journal of Biological Chemistry . 273: 24550-63. PMID 9733750 DOI: 10.1074/jbc.273.38.24550
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How a holoenzyme for DNA replication is formed
Jan 02, 2013 · Hingorani MM, O'Donnell M. ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme. J Biol Chem. 1998; 273 (38):24550–24563. [Google Scholar]
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Temporal Correlation of DNA Binding, ATP Hydrolysis, and
Sep 15, 2009 · Hingorani MM, O'Donnell M. ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme. J. Biol. Chem. 1998; 273:24550–24563. [Google Scholar]
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Initiation Complex Formation, Mechanism of | SpringerLink
Jan 30, 2018 · Hingorani MM, O'Donnell ME (1998) ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme. J Biol Chem 273:24550–24563 PubMed CrossRef Google Scholar
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RCSB PDB - 1XXI: ADP Bound E. coli Clamp Loader Complex
Nov 05, 2004 · Clamp-loader complexes are heteropentameric AAA+ ATPases that load sliding clamps onto DNA. The structure of the nucleotide-free Escherichia coli clamp loader had been determined previously and led to the proposal that the clamp-loader cycles between an inactive state, in which the ATPase domains form a closed ring, and an active state that opens up to …
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Michael E. O'Donnell - Publications
ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme. The Journal of Biological Chemistry . 273: 24550-63. PMID 9733750 DOI: 10.1074/jbc.273.38.24550
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Kinetic analysis of PCNA clamp binding and release in the
Jan 01, 2015 · ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme J. Biol. Chem., 273 ( 1998 ), pp. 24550 - 24563 Article Download PDF View Record in Scopus Google Scholar
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THE J B C Vol. 273, No. 38, Issue of September 18, …
The action of ATP-dependent clamp loader complexes is required to open the circular clamps and to load them onto DNA. The crystal structure of the pentameric clamp loader complex from Escherichia coli (the gamma complex), determined in the absence of nucleotides, revealed a highly asymmetric and extended form of the clamp loader.
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Distinct roles for ATP binding and hydrolysis at
Mar 11, 2004 · Hingorani MM, O'Donnell M (1998) ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme. J Biol Chem 273: 24550 – 24563 Crossref CAS PubMed Web of Science® Google Scholar; Jarvis TC, Paul LS, von Hippel PH (1989) Structural and enzymatic studies of the T4 DNA replication
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ATP Binding to the Escherichia coli Clamp Loader Powers
Sep 18, 1998 · The E. coli clamp loader, γ complex, is a composite of five different proteins, γ, δ, δ′, χ, and ψ, of which γ is the ATP-binding subunit essential for clamp loading (4, 5, 6, 7). The clamp, β, is a dimeric ring with a 35-Å inner diameter, large enough to encircle DNA ( 8 ). β and γ complex form part of DNA polymerase III holoenzyme, the replicative DNA polymerase of E. coli .
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Structure of the human clamp loader reveals an
Sep 09, 2020 · , Mechanism of loading the Escherichia coli DNA polymerase III beta sliding clamp on DNA. Bona fide primer/templates preferentially trigger the gamma complex to hydrolyze ATP and load the clamp. J. Biol. Chem. 278, 10033 – 10040 (2003).
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ATP Binding to the Escherichia coli Clamp Loader Powers Opening of the Ring-shaped Clamp of DNA Polymerase III Holoenzyme October 1998 Journal of Biological Chemistry 273(38):24550-63
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ATP Binding to the Escherichia coli Clamp Loader Powers
The Escherichia coli gamma complex serves as a clamp loader, catalyzing ATP-dependent assembly of beta protein clamps onto primed DNA templates during DNA replication.
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The clamp-loading complex for processive DNA replication
Jun 20, 2004 · A clamp loader complex loads such clamps onto the DNA strand by opening the clamp ring while at the same time binding and hydrolyzing ATP. All of the sliding clamps, including the Escherichia coli
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(PDF) ATP Binding to the Escherichia coli Clamp Loader
The Escherichia coli g complex serves as a clamp loader, catalyzing ATP-dependent assembly of bprotein clamps onto primed DNA templates during DNA repli-cation. These ring-shaped clamps tether DNA polymer-ase III holoenzyme to the template, facilitating rapid and processive DNA synthesis. This report focuses on
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ATP binding to the Escherichia coli clamp loader powers
The E. coli clamp loader functions as a "protein topoisomerase," cracking open the ring-shaped β clamp to place DNA in the center of the ring. ATP binding powers changes in γ complex that lead to formation of a γ complex·open β ring·DNA composite, which is likely an important intermediate in the clamp loading pathway.
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Structure of the ATP synthase catalytic complex (F1) from
ATP synthase is a membrane-bound, rotary motor enzyme that is critical for cellular energy metabolism in all kingdoms of life. Despite conservation of its basic structure and function, auto-inhibition by one of its rotary stalk subunits occurs in bacteria
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Fluorescence measurements on the E.coli DNA …
Jan 11, 2013 · Abstract. Escherichia coliγ complex clamp loader functions to load the β sliding clamp onto sites of DNA replication and repair. The clamp loader uses the energy of ATP binding and hydrolysis to drive conformational changes allowing for β binding and opening, DNA binding, and then release of the β·DNA complex.
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