Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center - Test2 - elhamkhani - TriplyDB

Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center

Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center

http://www.wikidata.org/entity/Q27621859

about

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 gyrase Structure of the N-terminal Gyrase B fragment in complex with ADP⋅Pi reveals rigid-body motion induced by ATP hydrolysis Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism Structure of rat BCKD kinase: Nucleotide-induced domain communication in a mitochondrial protein kinase An open conformation of the Thermus thermophilus gyrase B ATP-binding domain Structure 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-187 Crystal structure of DNA gyrase B' domain sheds lights on the mechanism for T-segment navigation Structure of a topoisomerase II–DNA–nucleotide complex reveals a new control mechanism for ATPase activity Structure of an 'open' clamp type II topoisomerase-DNA complex provides a mechanism for DNA capture and transport Direct control of type IIA topoisomerase activity by a chromosomally encoded regulatory protein Mycobacterium tuberculosis DNA gyrase ATPase domain structures suggest a dissociative mechanism that explains how ATP hydrolysis is coupled to domain motion Biophysical highlights from 54 years of macromolecular crystallography Molecular cloning of apicoplast-targeted Plasmodium falciparum DNA gyrase genes: unique intrinsic ATPase activity and ATP-independent dimerization of PfGyrB subunit.Overview of protein structural and functional folds.Characterization of the interaction between DNA gyrase inhibitor and DNA gyrase of Escherichia coli.Crystallization and X-ray diffraction data collection of topoisomerase IV ParE subunit from Xanthomonas oryzae pv. oryzae.Contribution of the ATP binding site of ParE to susceptibility to novobiocin and quinolones in Streptococcus pneumoniae New mutation in parE in a pneumococcal in vitro mutant resistant to fluoroquinolones.Genetic analyses of mutations contributing to fluoroquinolone resistance in clinical isolates of Streptococcus pneumoniae Exploiting bacterial DNA gyrase as a drug target: current state and perspectives.Hsp90: chaperoning signal transduction.Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone.Structure of adeno-associated virus type 2 Rep40-ADP complex: insight into nucleotide recognition and catalysis by superfamily 3 helicases Solution structures of DNA-bound gyrase.ATPases as drug targets: learning from their structure.Potassium ions are required for nucleotide-induced closure of gyrase N-gate Functional Analyses of the Toxoplasma gondii DNA Gyrase Holoenzyme: A Janus Topoisomerase with Supercoiling and Decatenation Abilities.ATP-bound conformation of topoisomerase IV: a possible target for quinolones in Streptococcus pneumoniae Coupling between ATP binding and DNA cleavage by DNA topoisomerase II: A unifying kinetic and structural mechanism.Purification, crystallization and preliminary X-ray crystallographic studies of the Mycobacterium tuberculosis DNA gyrase ATPase domain.Structural insight into negative DNA supercoiling by DNA gyrase, a bacterial type 2A DNA topoisomerase Crystallization and preliminary crystallographic studies of Mycobacterium tuberculosis DNA gyrase B C-terminal domain, part of the enzyme reaction core.A "Double-Edged" Scaffold: Antitumor Power within the Antibacterial Quinolone.Structural frameworks for considering microbial protein- and nucleic acid-dependent motor ATPases.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.Biological evaluation of benzothiazole ethyl urea inhibitors of bacterial type II topoisomerases.Squaring up to DNA: pentapeptide repeat proteins and DNA mimicry.Exploration of fluoroquinolone resistance in Streptococcus pyogenes: comparative structure analysis of wild-type and mutant DNA gyrase.

P2860

Q24567584-263171B5-EC2B-439E-8DCB-6E50327D2460 Q27347826-91424E34-D080-42CB-B815-D4392EFC94BE Q27633990-E8381192-7479-4A15-BA13-258E25A8E4D1 Q27634871-E72D0562-2643-45E2-8421-C199F41888C7 Q27637851-6068CE63-A4C4-422D-B77C-21C40409D96E Q27640255-D60E4254-D136-4573-80F8-712028DA3EF7 Q27641998-8761BD16-5821-48AF-A10D-BD79CE30D662 Q27656386-824D550B-87C1-4683-914D-0EFD4EBCE36B Q27673758-B3333B09-DC9E-4B57-8B68-900771AD5699 Q27679776-37D847B2-BE30-4191-84FE-2B11628E0984 Q27684534-A4339825-9C88-486E-9E07-3328C575C469 Q27685473-8C7CF9E0-8BEC-49D1-8E6A-B03E29FEFE72 Q28658133-72A9FF34-5A78-44C9-9D3D-0E0A2FD7A21F Q30042495-D9545DD0-3BFB-4F02-9141-D59D39E3975A Q30368988-85E03FA4-EC29-4795-AC21-53381A321D87 Q33289415-BA34C9E9-56C3-4E85-B0D9-321CACC60B94 Q33455379-08D339EA-A40A-44EF-947D-F81ED293D59F Q33757558-F171FC31-FA78-46B0-91BE-318951E00C55 Q33981750-09868F75-ADCB-408F-82CF-B4EDA2F22DF2 Q33983643-26D32875-6712-4B92-B59F-31C3D62BB3AB Q34214929-43DB1640-1B2D-498B-875B-5F3BEAA926B3 Q34319594-2D31D39F-41AF-4823-9EF1-936AA794B0BD Q34338453-056C59E3-0037-49C9-AC1D-F20953011570 Q34341088-B7463E13-F4F5-4F48-895C-1F4B313CD821 Q34513886-55DF3B7C-F357-4E92-A5D5-5F6A6893FDC6 Q34810356-3FF7248F-E2C7-4E89-9F00-6B61313B4E28 Q35879426-02DA2B59-EB22-4407-9CDA-D25C9D5C858F Q36100114-BE988C53-3347-4A53-BD94-2252DE59442D Q36474350-658583BD-183B-47E7-89F7-3EC890FA8578 Q36719248-FDECC53A-57C3-4D5C-9A95-923499179559 Q36890089-61B5EEB2-7A9A-4307-8F81-FE880ED73BCE Q37148510-9AEC3287-AA6D-4F3A-A440-AF27B9BCD3FE Q37148807-94758522-B794-432F-96A8-291F9585A703 Q37204002-005FC3FB-950C-42FE-B4E7-6B881A93FCFB Q37223884-82377E38-0239-4EE5-A79C-681EA41842AA Q37255381-65AF7649-66B9-4C79-B348-DCC5B7B77ECF Q37304105-967EFCCF-2E26-4ED4-89E0-E743A92E91AC Q37335706-FF97BACB-07C7-4FDA-9266-D39E8C1730EE Q38262589-8CEA282B-FFA3-4F36-898C-AE5C7E68ADD7 Q38408892-A0077E60-DF7A-44CB-A5BA-C1D6BDC80C93

P2860

Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center

http://www.wikidata.org/entity/Q27621859

description

2000 nî lūn-bûn

@nan

2000 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի մարտին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

Dimerization of Escherichia co ...... ng the ATPase catalytic center

@ast

Dimerization of Escherichia co ...... ng the ATPase catalytic center

@en

Dimerization of Escherichia co ...... ng the ATPase catalytic center

@nl

type

label

Dimerization of Escherichia co ...... ng the ATPase catalytic center

@ast

Dimerization of Escherichia co ...... ng the ATPase catalytic center

@en

Dimerization of Escherichia co ...... ng the ATPase catalytic center

@nl

prefLabel

Dimerization of Escherichia co ...... ng the ATPase catalytic center

@ast

Dimerization of Escherichia co ...... ng the ATPase catalytic center

@en

Dimerization of Escherichia co ...... ng the ATPase catalytic center

@nl

P1433

Q27621859-FCD4BA6E-527A-4C7A-A8B5-F2B2157057D2

P1476

Q27621859-B27973D1-FE64-4898-99D8-8E69D054D724

P2093

Q27621859-0C2DCF7C-27F0-4E40-BFA7-70087FB87D23

Q27621859-0F493B1F-1B5E-40B7-BFB3-0D7E091DCA41

Q27621859-2A017B4A-768C-41DF-B7EC-076C6C53B28E

Q27621859-59A31027-4D65-4DF7-B18E-22A94E557488

Q27621859-65796EDA-0536-44A0-A50F-E0BBC6089603

Q27621859-86138403-717C-4086-9022-F63B161DD602

Q27621859-FD94F974-39B2-45FE-9AFA-3A6BC9F61BAF

P2860

Q27621859-06E366A8-882F-4853-8F8D-8A224F21B5F7

Q27621859-0BDDAB04-1F42-43B4-9378-D9D3E5760B98

Q27621859-1A5925EC-DFC7-4BB0-B0F0-EE75C86E9991

Q27621859-1F03A329-0718-4EAB-842B-0EDB72376C34

Q27621859-2839FEBD-59B3-4CB6-848A-B8A21ACEE774

Q27621859-400FA937-EAE7-4E91-9241-51DA643E11E2

Q27621859-41BAF937-0263-4D6F-BDCB-D72131E943A9

Q27621859-5322AC81-23CA-4824-AC61-BE7AA0F72640

Q27621859-68C0F859-0FED-4335-A029-29F2692F17FA

Q27621859-6D014EC5-9718-4C3F-97E6-C6216768D84B

P304

Q27621859-02D6AC5F-EAF8-43EA-9F5F-C1E8B7A8FBF3

P31

Q27621859-B7D24C1C-3988-4CB2-8715-9DEBE057AEDB

P3181

Q27621859-8BD69872-7802-4571-83B6-AA96A4637B31

P356

Q27621859-9197E23C-ED5D-4499-8FAF-94A06AB913FF

P407

Q27621859-05D527B2-0361-423F-8422-4BD4E527269E

P433

Q27621859-A89F4DF9-CDDA-4513-BD5B-DC1593D110E5

P478

Q27621859-C09BF229-5DF2-4E9F-B865-5D682FE438EA

P577

Q27621859-DCFC348E-12CE-46E4-96B0-EFBE8F8AD684

P5875

Q27621859-58548A23-B946-4873-9631-F4820094A6FF

P698

Q27621859-8923C921-6034-42A6-8F57-55FB9ADA10ED

P921

Q27621859-4E82C305-0647-4C94-AFD3-67303082278C

P3181

P356

JBC.275.13.9468

P1433

Journal of Biological Chemistry

P1476

Dimerization of Escherichia co ...... ng the ATPase catalytic center

@en

P2093

A Mitschler

http://www.w3.org/2001/XMLSchema#string

A Urzhumtsev

http://www.w3.org/2001/XMLSchema#string

C Bronner

http://www.w3.org/2001/XMLSchema#string

D Moras

http://www.w3.org/2001/XMLSchema#string

L Brino

http://www.w3.org/2001/XMLSchema#string

M Mousli

http://www.w3.org/2001/XMLSchema#string

P Oudet

http://www.w3.org/2001/XMLSchema#string

P2860

PROMOTIF--a program to identify and analyze structural motifs in proteins

Improved methods for building protein models in electron density maps and the location of errors in these models

Structure and mechanism of DNA topoisomerase II

SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

xdlMAPMAN and xdlDATAMAN - programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets

AMoRe: an automated package for molecular replacement

DNA gyrase: an enzyme that introduces superhelical turns into DNA.

Crystal structure of an N-terminal fragment of the DNA gyrase B protein.

DNA gyrase: structure and function.

Energy coupling in DNA gyrase and the mechanism of action of novobiocin.

P304

9468-75

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

3932495

http://www.w3.org/2001/XMLSchema#string

P356

10.1074/JBC.275.13.9468

http://www.w3.org/2001/XMLSchema#string

P407

P433

13

http://www.w3.org/2001/XMLSchema#string

P478

275

http://www.w3.org/2001/XMLSchema#string

P577

2000-03-31T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

279240683

http://www.w3.org/2001/XMLSchema#string

P698

10734094

http://www.w3.org/2001/XMLSchema#string

P921

Escherichia coli