A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias.
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Breakage-reunion domain of Streptococcus pneumoniae topoisomerase IV: crystal structure of a gram-positive quinolone targetCrystal structure of DNA gyrase B' domain sheds lights on the mechanism for T-segment navigationA 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 EFFICIENCYStructural basis for the MukB-topoisomerase IV interaction and its functional implicationsin vivoMycobacterium tuberculosis DNA gyrase possesses two functional GyrA-boxesInvestigating the Roles of the C-Terminal Domain of Plasmodium falciparum GyrAMechanochemical analysis of DNA gyrase using rotor bead tracking.Species-specific supercoil dynamics of the bacterial nucleoid.Twisting of the DNA-binding surface by a beta-strand-bearing proline modulates DNA gyrase activity.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.Subnuclear domain proteins in cancer cells support the functions of RUNX2 in the DNA damage response.All tangled up: how cells direct, manage and exploit topoisomerase function.Local sensing of global DNA topology: from crossover geometry to type II topoisomerase processivityUnique features of apicoplast DNA gyrases from Toxoplasma gondii and Plasmodium falciparum.Guiding strand passage: DNA-induced movement of the gyrase C-terminal domains defines an early step in the supercoiling cycleMechanisms 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.Chiral discrimination and writhe-dependent relaxation mechanism of human topoisomerase IIα.Bimodal recognition of DNA geometry by human topoisomerase II alpha: preferential relaxation of positively supercoiled DNA requires elements in the C-terminal domainStructural insight into negative DNA supercoiling by DNA gyrase, a bacterial type 2A DNA topoisomeraseDNA topoisomerases: harnessing and constraining energy to govern chromosome topology.Engineering new protein-protein interactions on the β-propeller fold by yeast cell surface displayDistinct regions of the Escherichia coli ParC C-terminal domain are required for substrate discrimination by topoisomerase IV.Quinolones: action and resistance updated.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.Molecular characterization of fluoroquinolone-resistant Moraxella catarrhalis variants generated in vitro by stepwise selection.Purification, crystallization and preliminary X-ray crystallographic studies of the Mycobacterium tuberculosis DNA gyrase CTDStructural Dynamics and Mechanochemical Coupling in DNA Gyrase.Formation of a wrapped DNA-protein interface: experimental characterization and analysis of the large contributions of ions and water to the thermodynamics of binding IHF to H' DNA.Probing the differential interactions of quinazolinedione PD 0305970 and quinolones with gyrase and topoisomerase IVBinding of two DNA molecules by type II topoisomerases for decatenation.ATP binding controls distinct structural transitions of Escherichia coli DNA gyrase in complex with DNA.DNA gyrase from the albicidin producer Xanthomonas albilineans has multiple-antibiotic-resistance and unusual enzymatic properties.Molecular modeling of Mycobacterium tuberculosis DNA gyrase and its molecular docking study with gatifloxacin inhibitors.Topoisomerase action on short DNA duplexes reveals requirements for gate and transfer DNA segments.Multiple modes of Escherichia coli DNA gyrase activity revealed by force and torque.The "GyrA-box" is required for the ability of DNA gyrase to wrap DNA and catalyze the supercoiling reaction.
P2860
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P2860
A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
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2005年學術文章
@zh-hant
name
A superhelical spiral in the E ...... directional supercoiling bias.
@en
A superhelical spiral in the E ...... directional supercoiling bias.
@nl
type
label
A superhelical spiral in the E ...... directional supercoiling bias.
@en
A superhelical spiral in the E ...... directional supercoiling bias.
@nl
prefLabel
A superhelical spiral in the E ...... directional supercoiling bias.
@en
A superhelical spiral in the E ...... directional supercoiling bias.
@nl
P2093
P2860
P356
P1476
A superhelical spiral in the E ...... idirectional supercoiling bias
@en
P2093
Daina M Graybosch
Gregory L Verdine
John C Huetsch
P2860
P304
26177-26184
P356
10.1074/JBC.M502838200
P407
P577
2005-05-15T00:00:00Z