메뉴 건너뛰기




Volumn 9, Issue 9, 2014, Pages

Structure of the N-Terminal Gyrase B fragment in complex with ADP?Pi reveals rigid-body motion induced by ATP hydrolysis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; DNA TOPOISOMERASE (ATP HYDROLYSING); DNA TOPOISOMERASE (ATP HYDROLYSING) B; ADENOSINE TRIPHOSPHATASE; DNA SUPERCOILING; ESCHERICHIA COLI PROTEIN; PERIODATE-OXIDIZED ADP;

EID: 84927631269     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0107289     Document Type: Article
Times cited : (52)

References (33)
  • 1
    • 2442599792 scopus 로고    scopus 로고
    • Structure, molecular mechanisms, and evolutionary relationships in DNA topoisomerases
    • Corbett KD, Berger JM (2004) Structure, molecular mechanisms, and evolutionary relationships in DNA topoisomerases. Annu Rev Biophys Biomol Struct 33: 95-118.
    • (2004) Annu Rev Biophys Biomol Struct , vol.33 , pp. 95-118
    • Corbett, K.D.1    Berger, J.M.2
  • 2
    • 50649101663 scopus 로고    scopus 로고
    • DNA topoisomerases: Harnessing and constraining energy to govern chromosome topology
    • Schoeffler AJ, Berger JM (2008) DNA topoisomerases: harnessing and constraining energy to govern chromosome topology. Q Rev Biophys 41: 41-101.
    • (2008) Q Rev Biophys , vol.41 , pp. 41-101
    • Schoeffler, A.J.1    Berger, J.M.2
  • 3
    • 77953417294 scopus 로고    scopus 로고
    • Front of and behind the replication fork: Bacterial type IIA topoisomerases
    • Sissi C, Palumbo M (2010) In front of and behind the replication fork: bacterial type IIA topoisomerases. Cell Mol Life Sci 67: 2001-2024.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 2001-2024
    • Sissi, C.1    Palumbo, M.2
  • 4
    • 80055065448 scopus 로고    scopus 로고
    • The ancestral role of ATP hydrolysis in type II topoisomerases: Prevention of DNA double-strand breaks
    • Bates AD, Berger JM, Maxwell A (2011) The ancestral role of ATP hydrolysis in type II topoisomerases: prevention of DNA double-strand breaks. Nucleic Acids Res 39: 6327-6339.
    • (2011) Nucleic Acids Res , vol.39 , pp. 6327-6339
    • Bates, A.D.1    Berger, J.M.2    Maxwell, A.3
  • 5
    • 84894348243 scopus 로고    scopus 로고
    • The mechanism of negative DNA supercoiling: A cascade of DNA-induced conformational changes prepares gyrase for strand passage
    • Gubaev A, Klostermeier D (2014) The mechanism of negative DNA supercoiling: A cascade of DNA-induced conformational changes prepares gyrase for strand passage. DNA Repair (Amst) 16C: 23-34.
    • (2014) DNA Repair (Amst) , vol.16 , pp. 23-34
    • Gubaev, A.1    Klostermeier, D.2
  • 6
    • 0026428621 scopus 로고
    • Crystal structure of an N-Terminal fragment of the DNA gyrase B protein
    • Wigley DB, Davies GJ, Dodson EJ, Maxwell A, Dodson G (1991) Crystal structure of an N-Terminal fragment of the DNA gyrase B protein. Nature 351: 624-629.
    • (1991) Nature , vol.351 , pp. 624-629
    • Wigley, D.B.1    Davies, G.J.2    Dodson, E.J.3    Maxwell, A.4    Dodson, G.5
  • 7
    • 0027419771 scopus 로고
    • The 43-kilodalton N-Terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs
    • Ali JA, Jackson AP, Howells AJ, Maxwell A (1993) The 43-kilodalton N-Terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs. Biochemistry 32: 2717-2724.
    • (1993) Biochemistry , vol.32 , pp. 2717-2724
    • Ali, J.A.1    Jackson, A.P.2    Howells, A.J.3    Maxwell, A.4
  • 8
    • 80052181150 scopus 로고    scopus 로고
    • DNA-induced narrowing of the gyrase N-gate coordinates T-segment capture and strand passage
    • Gubaev A, Klostermeier D (2011) DNA-induced narrowing of the gyrase N-gate coordinates T-segment capture and strand passage. Proc Natl Acad Sci USA 108: 14085-14090.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 14085-14090
    • Gubaev, A.1    Klostermeier, D.2
  • 9
    • 0032493388 scopus 로고    scopus 로고
    • Identification of a residue involved in transitionstate stabilization in the ATPase reaction of DNA gyrase
    • Smith CV, Maxwell A (1998) Identification of a residue involved in transitionstate stabilization in the ATPase reaction of DNA gyrase. Biochemistry 37: 9658-9667.
    • (1998) Biochemistry , vol.37 , pp. 9658-9667
    • Smith, C.V.1    Maxwell, A.2
  • 10
    • 0037413727 scopus 로고    scopus 로고
    • Structure of the topoisomerase VI-B subunit: Implications for type II topoisomerase mechanism and evolution
    • Corbett KD, Berger JM (2003) Structure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolution. EMBO J 22: 151-163.
    • (2003) EMBO J , vol.22 , pp. 151-163
    • Corbett, K.D.1    Berger, J.M.2
  • 11
    • 20444401591 scopus 로고    scopus 로고
    • Structural dissection of ATP turnover in the prototypical GHL ATPase TopoVI
    • Corbett KD, Berger JM (2005) Structural dissection of ATP turnover in the prototypical GHL ATPase TopoVI. Structure 13: 873-882.
    • (2005) Structure , vol.13 , pp. 873-882
    • Corbett, K.D.1    Berger, J.M.2
  • 12
    • 27744591551 scopus 로고    scopus 로고
    • Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase
    • Wei H, Ruthenburg AJ, Bechis SK, Verdine GL (2005) Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase. J Biol Chem 280: 37041-37047.
    • (2005) J Biol Chem , vol.280 , pp. 37041-37047
    • Wei, H.1    Ruthenburg, A.J.2    Bechis, S.K.3    Verdine, G.L.4
  • 13
    • 0034737716 scopus 로고    scopus 로고
    • Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center
    • Brino L, Urzhumtsev A, Mousli M, Bronner C, Mitschler A, et al. (2000) Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center. J Biol Chem 275: 9468-9475.
    • (2000) J Biol Chem , vol.275 , pp. 9468-9475
    • Brino, L.1    Urzhumtsev, A.2    Mousli, M.3    Bronner, C.4    Mitschler, A.5
  • 14
    • 70449768051 scopus 로고    scopus 로고
    • The MORPHEUS protein crystallization screen
    • Gorrec F (2009) The MORPHEUS protein crystallization screen. J Appl Crystallogr 42: 1035-1042.
    • (2009) J Appl Crystallogr , vol.42 , pp. 1035-1042
    • Gorrec, F.1
  • 23
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • Kleywegt GJ (1996) Use of non-crystallographic symmetry in protein structure refinement. Acta Crystallogr D Biol Crystallogr 52: 842-857.
    • (1996) Acta Crystallogr D Biol Crystallogr , vol.52 , pp. 842-857
    • Kleywegt, G.J.1
  • 24
    • 79251615811 scopus 로고    scopus 로고
    • Efficient enzymatic production of the bacterial second messenger c-di-GMP by the diguanylate cyclase YdeH from e
    • Zahringer F, Massa C, Schirmer T (2011) Efficient enzymatic production of the bacterial second messenger c-di-GMP by the diguanylate cyclase YdeH from E. coli. Appl Biochem Biotechnol 163: 71-79.
    • (2011) Coli Appl Biochem Biotechnol , vol.163 , pp. 71-79
    • Zahringer, F.1    Massa, C.2    Schirmer, T.3
  • 25
    • 84887448891 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis DNA gyrase ATPase domain structures suggest a dissociative mechanism that explains how ATP hydrolysis is coupled to domain motion
    • Agrawal A, Roué M, Spitzfaden C, Petrella S, Aubry A, et al. (2013) Mycobacterium tuberculosis DNA gyrase ATPase domain structures suggest a dissociative mechanism that explains how ATP hydrolysis is coupled to domain motion. Biochem J 456: 263-273.
    • (2013) Biochem J , vol.456 , pp. 263-273
    • Agrawal, A.1    Roué, M.2    Spitzfaden, C.3    Petrella, S.4    Aubry, A.5
  • 26
    • 17044438607 scopus 로고    scopus 로고
    • Crystallographic evidence for substrate-Assisted GTP hydrolysis by a small GTP binding protein
    • Pasqualato S, Cherfils J (2005) Crystallographic evidence for substrate-Assisted GTP hydrolysis by a small GTP binding protein. Structure 13: 533-540.
    • (2005) Structure , vol.13 , pp. 533-540
    • Pasqualato, S.1    Cherfils, J.2
  • 27
    • 33749014394 scopus 로고    scopus 로고
    • A phosphoryl transfer intermediate in the GTPase reaction of Ras in complex with its GTPase-Activating protein
    • Kötting C, Blessenohl M, Suveyzdis Y, Goody RS, Wittinghofer A, et al. (2006) A phosphoryl transfer intermediate in the GTPase reaction of Ras in complex with its GTPase-Activating protein. Proc Natl Acad Sci USA 103: 13911-13916.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13911-13916
    • Kötting, C.1    Blessenohl, M.2    Suveyzdis, Y.3    Goody, R.S.4    Wittinghofer, A.5
  • 28
    • 34447323073 scopus 로고    scopus 로고
    • Energy coupling in type II topoisomerases: Why do they hydrolyze ATP?
    • Bates AD, Maxwell A (2007) Energy coupling in type II topoisomerases: why do they hydrolyze ATP? Biochemistry 46: 7929-7941.
    • (2007) Biochemistry , vol.46 , pp. 7929-7941
    • Bates, A.D.1    Maxwell, A.2
  • 30
    • 33947147592 scopus 로고    scopus 로고
    • Dissection of the nucleotide cycle of B-subtilis DNA gyrase and its modulation by DNA
    • Goettler T, Klostermeier D (2007) Dissection of the nucleotide cycle of B-subtilis DNA gyrase and its modulation by DNA. J Mol Biol 367: 1392-1404.
    • (2007) J Mol Biol , vol.367 , pp. 1392-1404
    • Goettler, T.1    Klostermeier, D.2
  • 31
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter IR (2001) The Guanine Nucleotide-Binding Switch in Three Dimensions. Science 294: 1299-1304.
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1
  • 32
    • 67650090649 scopus 로고    scopus 로고
    • The QTK loop is essential for the communication between the N-Terminal atpase domain and the central cleavage-ligation region in human topoisomerase IIalpha
    • Bendsen S, Oestergaard VH, Skouboe C, Brinch M, Knudsen BR, et al. (2009) The QTK loop is essential for the communication between the N-Terminal atpase domain and the central cleavage-ligation region in human topoisomerase IIalpha. Biochemistry 48: 6508-6515.
    • (2009) Biochemistry , vol.48 , pp. 6508-6515
    • Bendsen, S.1    Oestergaard, V.H.2    Skouboe, C.3    Brinch, M.4    Knudsen, B.R.5
  • 33
    • 0021715525 scopus 로고
    • The DNA dependence of the ATPase activity of DNA gyrase
    • Maxwell A, Gellert M (1984) The DNA dependence of the ATPase activity of DNA gyrase. Journal of Biological Chemistry 259: 14472-14480.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 14472-14480
    • Maxwell, A.1    Gellert, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.