The role of monovalent cations in the ATPase reaction of DNA gyrase

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The role of monovalent cations in the ATPase reaction of DNA gyrase is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1107/S1399004715002916
P932PMC publication ID4388272
P698PubMed publication ID25849408

P50authorAnthony MaxwellQ37380949
P2093author name stringDavid Mark Lawson
Clare Elizabeth Mary Stevenson
Stephen James Hearnshaw
Terence Tsz-Hong Chung
P2860cites workCellular roles of dna topoisomerases: a molecular perspectiveQ22121990
Crystal structures of Escherichia coli topoisomerase IV ParE subunit (24 and 43 kilodaltons): a single residue dictates differences in novobiocin potency against topoisomerase IV and DNA gyraseQ24567584
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Structure of the N-terminal Gyrase B fragment in complex with ADP⋅Pi reveals rigid-body motion induced by ATP hydrolysisQ27347826
Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic centerQ27621859
Structure of rat BCKD kinase: Nucleotide-induced domain communication in a mitochondrial protein kinaseQ27634871
An open conformation of the Thermus thermophilus gyrase B ATP-binding domainQ27637851
Structure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolutionQ27640255
Monovalent cation dependence and preference of GHKL ATPases and kinasesQ27641375
Structure of the topoisomerase II ATPase region and its mechanism of inhibition by the chemotherapeutic agent ICRF-187Q27641998
Atomic structure of the actin:DNase I complexQ27685392
How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active siteQ27730342
Coot: model-building tools for molecular graphicsQ27860505
Molecular replacement with MOLREPQ27860539
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Overview of the CCP4 suite and current developmentsQ27860782
Optimal description of a protein structure in terms of multiple groups undergoing TLS motionQ27860825
REFMAC5 for the refinement of macromolecular crystal structuresQ27860905
Automated refinement of protein modelsQ27860928
The ATP-binding site of type II topoisomerases as a target for antibacterial drugsQ28207771
Structure-based design and mechanisms of allosteric inhibitors for mitochondrial branched-chain α-ketoacid dehydrogenase kinaseQ28291558
Presenting your structures: the CCP4mg molecular-graphics softwareQ29547443
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GHKL, an emergent ATPase/kinase superfamilyQ33818817
Exploiting bacterial DNA gyrase as a drug target: current state and perspectives.Q34214929
Crystal structure of an N-terminal fragment of the DNA gyrase B protein.Q34493198
Structure, molecular mechanisms, and evolutionary relationships in DNA topoisomerasesQ35771555
Potassium ions are required for nucleotide-induced closure of gyrase N-gateQ35879426
Identifying the catalytic residue of the ATPase reaction of DNA gyraseQ36697175
Structural Aspects of Metal Liganding to Functional Groups in ProteinsQ36968037
New mechanistic and functional insights into DNA topoisomerases.Q38089800
The nature of inhibition of DNA gyrase by the coumarins and the cyclothialidines revealed by X-ray crystallographyQ41064279
A solution for the best rotation to relate two sets of vectorsQ45034417
Preliminary crystallographic analysis of the ATP-hydrolysing domain of the Escherichia coli DNA gyrase B proteinQ45203137
Structural dissection of ATP turnover in the prototypical GHL ATPase TopoVI.Q46530498
Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase.Q46650258
The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs.Q52399144
Monovalent cations and inorganic phosphate alter branched-chain alpha-ketoacid dehydrogenase-kinase activity and inhibitor sensitivityQ67946148
Metal-ligand geometry relevant to proteins and in proteins: sodium and potassiumQ78009584
P433issuePt 4
P304page(s)996-1005
P577publication date2015-03-27
P1433published inActa Crystallographica Section D: Biological CrystallographyQ1933255
P1476titleThe role of monovalent cations in the ATPase reaction of DNA gyrase
P478volume71

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cites work (P2860)
Q89507389Calcium binding to a remote site can replace magnesium as cofactor for mitochondrial Hsp90 (TRAP1) ATPase activity
Q52335752Efficient use of single molecule time traces to resolve kinetic rates, models and uncertainties.
Q92718521Modulated control of DNA supercoiling balance by the DNA-wrapping domain of bacterial gyrase

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