Conversion of DNA gyrase into a conventional type II topoisomerase
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DNA gyrase, topoisomerase IV, and the 4-quinolonesA model for the mechanism of strand passage by DNA gyraseBreakage-reunion domain of Streptococcus pneumoniae topoisomerase IV: crystal structure of a gram-positive quinolone targetA domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase functionA naturally chimeric type IIA topoisomerase in Aquifex aeolicus highlights an evolutionary path for the emergence of functional paralogsMechanisms for Defining Supercoiling Set Point of DNA Gyrase Orthologs: II. THE SHAPE OF THE GyrA SUBUNIT C-TERMINAL DOMAIN (CTD) IS NOT A SOLE DETERMINANT FOR CONTROLLING SUPERCOILING EFFICIENCYMycobacterium tuberculosis DNA gyrase possesses two functional GyrA-boxesPhylogenomics of type II DNA topoisomerasesTopoisomerase IV, alone, unknots DNA in E. coliMechanochemical analysis of DNA gyrase using rotor bead tracking.The ancestral role of ATP hydrolysis in type II topoisomerases: prevention of DNA double-strand breaks.Interaction of the plasmid-encoded quinolone resistance protein Qnr with Escherichia coli DNA gyrase.Interactions of CcdB with DNA gyrase. Inactivation of Gyra, poisoning of the gyrase-DNA complex, and the antidote action of CcdA.Twisting of the DNA-binding surface by a beta-strand-bearing proline modulates DNA gyrase activity.The tail that wags the dog: topoisomerase IV ParC C-terminal domain controls strand passage activity through multipartite topology-dependent interactions with DNA.Thai ethnomedicinal plants as resistant modifying agents for combating Acinetobacter baumannii infectionsβ-Propeller blades as ancestral peptides in protein evolution.Vibrio cholerae ParE2 poisons DNA gyrase via a mechanism distinct from other gyrase inhibitorsEvolutionary twist on topoisomerases: conversion of gyrase to topoisomerase IV.Solution structures of DNA-bound gyrase.Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of the C-terminal domain of the GyrA subunit of DNA gyrase from Staphylococcus aureus strain Mu50.Origins of the machinery of recombination and sex.How do type II topoisomerases use ATP hydrolysis to simplify DNA topology beyond equilibrium? Investigating the relaxation reaction of nonsupercoiling type II topoisomerasesAll tangled up: how cells direct, manage and exploit topoisomerase function.Local sensing of global DNA topology: from crossover geometry to type II topoisomerase processivityGuiding strand passage: DNA-induced movement of the gyrase C-terminal domains defines an early step in the supercoiling cycleInhibition of gene expression and growth by antisense peptide nucleic acids in a multiresistant beta-lactamase-producing Klebsiella pneumoniae strainMechanisms for defining supercoiling set point of DNA gyrase orthologs: I. A nonconserved acidic C-terminal tail modulates Escherichia coli gyrase activity.The GyrA-box determines the geometry of DNA bound to gyrase and couples DNA binding to the nucleotide cycle.Both DNA gyrase and reverse gyrase are present in the hyperthermophilic bacterium Thermotoga maritima.Structural insight into negative DNA supercoiling by DNA gyrase, a bacterial type 2A DNA topoisomeraseDNA topoisomerases: harnessing and constraining energy to govern chromosome topology.Distinct regions of the Escherichia coli ParC C-terminal domain are required for substrate discrimination by topoisomerase IV.Quinolones: action and resistance updated.DNA gyrase can cleave short DNA fragments in the presence of quinolone drugs.A strand-passage conformation of DNA gyrase is required to allow the bacterial toxin, CcdB, to access its binding site.The key DNA-binding residues in the C-terminal domain of Mycobacterium tuberculosis DNA gyrase A subunit (GyrA).The acidic C-terminal tail of the GyrA subunit moderates the DNA supercoiling activity of Bacillus subtilis gyrase.Active-site residues of Escherichia coli DNA gyrase required in coupling ATP hydrolysis to DNA supercoiling and amino acid substitutions leading to novobiocin resistance.Purification, crystallization and preliminary X-ray crystallographic studies of the Mycobacterium tuberculosis DNA gyrase CTD
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Conversion of DNA gyrase into a conventional type II topoisomerase
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Conversion of DNA gyrase into a conventional type II topoisomerase
@en
Conversion of DNA gyrase into a conventional type II topoisomerase.
@nl
type
label
Conversion of DNA gyrase into a conventional type II topoisomerase
@en
Conversion of DNA gyrase into a conventional type II topoisomerase.
@nl
prefLabel
Conversion of DNA gyrase into a conventional type II topoisomerase
@en
Conversion of DNA gyrase into a conventional type II topoisomerase.
@nl
P2860
P356
P1476
Conversion of DNA gyrase into a conventional type II topoisomerase
@en
P2093
Kampranis SC
P2860
P304
14416-14421
P356
10.1073/PNAS.93.25.14416
P407
P577
1996-12-01T00:00:00Z