Crystal structure of the delta' subunit of the clamp
The crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III has been determined. Three consecutive domains in the structure are arranged in a C-shaped architecture. The N-terminal domain contains a nonfunctional nucleotide binding site. The catalytic compone …
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PDB-1sxj: Crystal Structure of the Eukaryotic Clamp Loader
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Crystal structure of the delta' subunit of the clamp
Oct 31, 1997 · The crystal structure of the δ′ subunit of the clamp-loader complex of E. coli DNA polymerase III has been determined. Three consecutive domains in the structure are arranged in a C-shaped architecture. The N-terminal domain contains a nonfunctional nucleotide binding site.
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RCSB PDB - 1JR3: Crystal Structure of the Processivity
Aug 10, 2001 · The gamma complex, an AAA+ ATPase, is the bacterial homolog of eukaryotic replication factor C (RFC) that loads the sliding clamp (beta, homologous to PCNA) onto DNA. The 2.7/3.0 A crystal structure of gamma complex reveals a pentameric arrangement of subunits, with stoichiometry delta':gamma(3):delta.
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Carboxyl-terminal domain III of the delta' subunit of the
Nov 02, 2001 · The delta and delta' subunits are essential components of the DNA polymerase III holoenzyme, required for assembly and function of the DnaX-complex clamp loader (tau2gammadeltadelta'chipsi). The x-ray crystal structure of delta' contains three structural domains (Guenther, B., Onrust, R., Sali, A., O'Donnell, M., and Kuriyan, J. (1997) Cell 91
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How a DNA Polymerase Clamp Loader Opens a Sliding Clamp
The extent of clamp opening seen in the crystal structure is likely to be close to that of the clamp–clamp loader complex prior to DNA binding because of extensive interactions between each of the five clamp loader subunits and the clamp, with the bound ATP stabilizing this conformation (see below).
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DNA clamp - Wikipedia
The beta clamp is a specific DNA clamp and a subunit of the DNA polymerase III holoenzyme found in bacteria. Two beta subunits are assembled around the DNA by the gamma subunit and ATP hydrolysis; this assembly is called the pre-initiation complex.After assembly around the DNA, the beta subunits' affinity for the gamma subunit is replaced by an affinity for the alpha and epsilon subunits
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Crystal structure of the DNA polymerase III β subunit (β
Feb 27, 2015 · The crystal structure of a β-clamp was first determined for E. coli in 1992, and after that for five other bacteria so far [6-8]. The structures show that the bacterial sliding clamp is a head-to-tail dimer, where one of the interfaces is opened by the clamp loader to allow DNA to enter the ring interior .
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Crystal Structure of the Processivity Clamp Loader …
The δ subunit of the γ complex binds to the β ring and opens it. The crystal structure of a β:δ complex shows that δ, which is structurally related to the δ′ and γ subunits of the γ complex, is a molecular wrench that induces or traps a conformational change in β such that one of its dimer interfaces is destabilized.
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NMR resonance assignments for the N-terminal domain of the
Mar 06, 2017 · X-ray crystal structures of the γ clamp loader complex (Jeruzalmi et al. 2001a; Simonetta et al. 2009), the closed β-clamp (Kong et al. 1992; Oakley et al. 2003) (Fig. 1a) and the β-clamp I272A/L273A monomer bound to the clamp loader δ subunit (Jeruzalmi et al. 2001b) (Fig. 1b) provided initial insights into the β-clamp loading process. For example, the β-clamp I272A/L273A mutant with a
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Crystal Structure of the δ′ Subunit of the Clamp-Loader
The crystal structure of the δ′ subunit of the clamp-loader complex of E. coli DNA polymerase III has been determined. Three consecutive domains in the structure are arranged in a C-shaped architecture. The N-terminal domain contains a nonfunctional nucleotide binding site. The catalytic component of the clamp-loader complex is the γ subunit, which is homologous to δ′. A sequence
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articles Structural analysis of a eukaryotic sliding DNA
the hydrolysis of ATPso that the complex is disassembled, the clamp is loaded onto DNA, and the clamp loader is released for another cycle of clamp loading10,18. We now describe the crystal structure of the S. cerevisiae RFC complex bound to the PCNA clamp. The structure reveals an unexpected ATP-dependent spiral arrangement of the ATPase
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Crystal structure of the chi:psi sub-assembly of the
Jan 01, 2004 · Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III. Guenther B, Onrust R, Sali A, O'Donnell M, Kuriyan J. Cell, 91(3):335-345, 01 Oct 1997 Cited by: 153 articles | PMID: 9363942
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Cell, Vol. 106, 417–428, August 24, 2001, Copyright 2001
Delta Subunit Wrench of the Clamp Loader Complex of E. coli DNA (homolog of eukaryotic Replication Factor C, otic PCNA and T4 gp45 are strikingly similar in structure RFC). The subunit of the complex binds to the to the clamp, but are trimers that have two rather than ring and opens it. The crystal structure of a : com-three domains in
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RCSB PDB - 1A5T: CRYSTAL STRUCTURE OF THE DELTA PRIME
The eukaryotic RFC is a complex consisting of one large and four small subunits. We have determined the crystal structure of the clamp loader small subunit (RFCS) from Pyrococcus furiosus. The six subunits, of which four bind ADP in their canonical nucleotide binding clefts, assemble into a dimer of semicircular trimers.
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A0A070VD07 | SWISS-MODEL Repository
assess : crystal structure of the delta prime subunit of the clamp-loader complex of escherichia coli dna po… homo-2-mer: 2× zn;
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PDB-1sxj: Crystal Structure of the Eukaryotic Clamp Loader
Delta Subunit Wrench of the Clamp Loader Complex of E. coli DNA (homolog of eukaryotic Replication Factor C, otic PCNA and T4 gp45 are strikingly similar in structure RFC). The subunit of the complex binds to the to the clamp, but are trimers that have two rather than ring and opens it. The crystal structure of a : com-three domains in
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holA - DNA polymerase III subunit delta - Escherichia coli
Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex (PubMed:2040637). DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3'-5' exonuclease activity.
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PDB-1sxj: Crystal Structure of the Eukaryotic Clamp Loader
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P28631 | SWISS-MODEL Repository
assess : crystal structure of the delta prime subunit of the clamp-loader complex of escherichia coli dna po… homo-2-mer: 2× zn;
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