Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase.
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A model for the mechanism of strand passage by DNA gyraseA monoclonal antibody that inhibits mycobacterial DNA gyrase by a novel mechanism.An open conformation of the Thermus thermophilus gyrase B ATP-binding domainStructure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolution.Structure of the topoisomerase II ATPase region and its mechanism of inhibition by the chemotherapeutic agent ICRF-187Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VIA domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase functionStructure of a topoisomerase II–DNA–nucleotide complex reveals a new control mechanism for ATPase activityMycobacterium tuberculosis DNA gyrase ATPase domain structures suggest a dissociative mechanism that explains how ATP hydrolysis is coupled to domain motionGene expression changes triggered by exposure of Haemophilus influenzae to novobiocin or ciprofloxacin: combined transcription and translation analysisThe ancestral role of ATP hydrolysis in type II topoisomerases: prevention of DNA double-strand breaks.DNA-induced narrowing of the gyrase N-gate coordinates T-segment capture and strand passageGuiding strand passage: DNA-induced movement of the gyrase C-terminal domains defines an early step in the supercoiling cycleE. coli Gyrase Fails to Negatively Supercoil Diaminopurine-Substituted DNA.Potassium ions are required for nucleotide-induced closure of gyrase N-gateThe GyrA-box determines the geometry of DNA bound to gyrase and couples DNA binding to the nucleotide cycle.DNA topoisomerases: harnessing and constraining energy to govern chromosome topology.The DNA-gate of Bacillus subtilis gyrase is predominantly in the closed conformation during the DNA supercoiling reaction.Single-molecule FRET reveals nucleotide-driven conformational changes in molecular machines and their link to RNA unwinding and DNA supercoiling.The additional 165 amino acids in the B protein of Escherichia coli DNA gyrase have an important role in DNA binding.Kinetic and thermodynamic analysis of mutant type II DNA topoisomerases that cannot covalently cleave DNA.The acidic C-terminal tail of the GyrA subunit moderates the DNA supercoiling activity of Bacillus subtilis gyrase.Functional characterisation of mycobacterial DNA gyrase: an efficient decatenase.Active-site residues of Escherichia coli DNA gyrase required in coupling ATP hydrolysis to DNA supercoiling and amino acid substitutions leading to novobiocin resistance.Interdomain communication in DNA topoisomerase II. DNA binding and enzyme activation.DNA gyrase with a single catalytic tyrosine can catalyze DNA supercoiling by a nicking-closing mechanism.Binding of two DNA molecules by type II topoisomerases for decatenation.A unique 45-amino-acid region in the toprim domain of Plasmodium falciparum gyrase B is essential for its activity.GyrI: a counter-defensive strategy against proteinaceous inhibitors of DNA gyrase.Hindering the strand passage reaction of human topoisomerase IIalpha without disturbing DNA cleavage, ATP hydrolysis, or the operation of the N-terminal clamp.Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase.The path of the DNA along the dimer interface of topoisomerase II.Topoisomerase VI senses and exploits both DNA crossings and bends to facilitate strand passage.Trapping of the transport-segment DNA by the ATPase domains of a type II topoisomerase.
P2860
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P2860
Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase.
@en
Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase.
@nl
type
label
Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase.
@en
Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase.
@nl
prefLabel
Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase.
@en
Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase.
@nl
P2860
P356
P1476
Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase.
@en
P2093
P2860
P304
P356
10.1093/NAR/24.24.4868
P407
P577
1996-12-01T00:00:00Z