메뉴 건너뛰기




Volumn 425, Issue 6956, 2003, Pages 419-423

A structural state of the myosin V motor without bound nucleotide

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; HYDROLYSIS; INTERFACES (MATERIALS);

EID: 0141732282     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01927     Document Type: Article
Times cited : (256)

References (30)
  • 1
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Holmes, K. C. & Geeves, M. A. Structural mechanism of muscle contraction. Annu. Rev. Biochem. 68, 687-728 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 687-728
    • Holmes, K.C.1    Geeves, M.A.2
  • 2
    • 0035312384 scopus 로고    scopus 로고
    • Myosin motors: Missing structures and hidden springs
    • Houdusse, A. & Sweeney, H. L. Myosin motors: missing structures and hidden springs. Curr. Opin. Struct. Biol. 11, 182-194 (2001).
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 182-194
    • Houdusse, A.1    Sweeney, H.L.2
  • 3
    • 0033527043 scopus 로고    scopus 로고
    • Myosin V is a processive actin-based motor
    • Mehta, A. D. E. et al. Myosin V is a processive actin-based motor. Nature 400, 590-593 (1999).
    • (1999) Nature , vol.400 , pp. 590-593
    • Mehta, A.D.E.1
  • 5
    • 0031149266 scopus 로고    scopus 로고
    • Myosin V-the multi-purpose transport motor
    • Titus, M. A. Myosin V-the multi-purpose transport motor. Curr. Biol. 7, R301-R304 (1997).
    • (1997) Curr. Biol. , vol.7
    • Titus, M.A.1
  • 7
    • 0032483563 scopus 로고    scopus 로고
    • Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: Visualization of the pre-power stroke state
    • Dominguez, R., Freyzon, Y. Trybus, K. M. & Cohen, C. Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. Cell 94, 559-571 (1998).
    • (1998) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 8
    • 1642340974 scopus 로고    scopus 로고
    • Atomic structure of scallop myosin subfragment S1 complexed with MgADP: A novel conformation of the myosin head
    • Houdusse, A., Kalabokis, V. N., Himmel, D., Szent-Gyorgyi, A. G. & Cohen, C. Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head. Cell 97, 459-470 (1999).
    • (1999) Cell , vol.97 , pp. 459-470
    • Houdusse, A.1    Kalabokis, V.N.2    Himmel, D.3    Szent-Gyorgyi, A.G.4    Cohen, C.5
  • 9
    • 0029176506 scopus 로고
    • A 35 Å movement of smooth muscle myosin on ADP release
    • Whittaker, M. et al. A 35 Å movement of smooth muscle myosin on ADP release. Nature 378, 748-751 (1995).
    • (1995) Nature , vol.378 , pp. 748-751
    • Whittaker, M.1
  • 11
    • 0037013903 scopus 로고    scopus 로고
    • Crystal structure of the motor domain of a class-1 myosin
    • Kollmar, M., Durrwang, U., Kliche, W., Manstein, D. J. & Kull, F. J. Crystal structure of the motor domain of a class-1 myosin. EMBO J. 21, 2517-2525 (2002).
    • (2002) EMBO J. , vol.21 , pp. 2517-2525
    • Kollmar, M.1    Durrwang, U.2    Kliche, W.3    Manstein, D.J.4    Kull, F.J.5
  • 12
    • 0027194702 scopus 로고
    • Three-dimensional structure of myosin subfragment-1: A molecular motor
    • Rayment, I. et al. Three-dimensional structure of myosin subfragment-1: A molecular motor. Science 261, 50-58 (1993).
    • (1993) Science , vol.261 , pp. 50-58
    • Rayment, I.1
  • 13
    • 0034624066 scopus 로고    scopus 로고
    • X-ray structures of the apo and MgATP-bound states of Dictyostelium discoideum myosin motor domain
    • Bauer, C. B., Holden, H. M., Thoden, J. B., Smith, R. & Rayment, I. X-ray structures of the apo and MgATP-bound states of Dictyostelium discoideum myosin motor domain. J. Biol. Chem. 275, 38494-38499 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 38494-38499
    • Bauer, C.B.1    Holden, H.M.2    Thoden, J.B.3    Smith, R.4    Rayment, I.5
  • 14
    • 0022404524 scopus 로고
    • Pressure-relaxation studies of pyrene-labelled actin and myosin subfragment-1 from rabbit skeletal muscle
    • Coates, J. H., Criddle, A. H. & Geeves, M. A. Pressure-relaxation studies of pyrene-labelled actin and myosin subfragment-1 from rabbit skeletal muscle. Biochem. 232, 351-356 (1985).
    • (1985) Biochem. , vol.232 , pp. 351-356
    • Coates, J.H.1    Criddle, A.H.2    Geeves, M.A.3
  • 15
    • 0034700284 scopus 로고    scopus 로고
    • Actin and light chain isoform dependence of myosin V kinetics
    • De La Cruz, E. M., Wells, A. L., Sweeney, H. L. & Ostap, E. M. Actin and light chain isoform dependence of myosin V kinetics. Biochemistry 39, 14196-14202 (2000).
    • (2000) Biochemistry , vol.39 , pp. 14196-14202
    • De La Cruz, E.M.1    Wells, A.L.2    Sweeney, H.L.3    Ostap, E.M.4
  • 16
    • 0026097954 scopus 로고
    • Kinetic studies on the association and dissociation of myosin subfragment 1 and actin
    • Taylor, E. W. Kinetic studies on the association and dissociation of myosin subfragment 1 and actin. J. Biol. Chem. 266, 294-302 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 294-302
    • Taylor, E.W.1
  • 17
    • 0034624082 scopus 로고    scopus 로고
    • Insertion or deletion of a single residue in the strut sequence of Dictyostelium myosin 11 abolishes strong binding to actin
    • Sasaki, N., Ohkura, R. & Sutoh, K. Insertion or deletion of a single residue in the strut sequence of Dictyostelium myosin 11 abolishes strong binding to actin. J. Biol. Chem. 275, 38705-38709 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 38705-38709
    • Sasaki, N.1    Ohkura, R.2    Sutoh, K.3
  • 18
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment, I. et al. Structure of the actin-myosin complex and its implications for muscle contraction. Science 261, 58-61 (1993).
    • (1993) Science , vol.261 , pp. 58-61
    • Rayment, I.1
  • 19
    • 0033669710 scopus 로고    scopus 로고
    • Evidence for cleft closure in actomyosin upon ADP release
    • Volkmann, N. et al. Evidence for cleft closure in actomyosin upon ADP release. Nature Struct. Biol. 7, 1147-1155 (2000).
    • (2000) Nature Struct. Biol. , vol.7 , pp. 1147-1155
    • Volkmann, N.1
  • 20
    • 0037025360 scopus 로고    scopus 로고
    • Actin-induced closure of the actin-binding cleft of smooth muscle myosin
    • Yengo, C. M., De La Cruz, E. M., Chrin, L. R., Gaffney, D. P. II & Berger, C. L. Actin-induced closure of the actin-binding cleft of smooth muscle myosin. J. Biol. Chem. 277, 24114-24119 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 24114-24119
    • Yengo, C.M.1    De La Cruz, E.M.2    Chrin, L.R.3    Gaffney D.P. II4    Berger, C.L.5
  • 21
    • 0036866606 scopus 로고    scopus 로고
    • Arf, Arl, Arp and Sar proteins: A family of GTP-binding proteins with a structural device for 'front-back' communication
    • Pasqualato, S., Renault, L. & Cherfils, J. Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication. EMBO Rep. 3, 1035-1041 (2002).
    • (2002) EMBO Rep. , vol.3 , pp. 1035-1041
    • Pasqualato, S.1    Renault, L.2    Cherfils, J.3
  • 22
    • 0033621469 scopus 로고    scopus 로고
    • Deletion of the myopathy loop of Dictyostelium myosin II and its impact on motor functions
    • Sasaki, N., Asukagawa, H., Yasuda, R., Hiratsuka, T. & Sutoh, K. Deletion of the myopathy loop of Dictyostelium myosin II and its impact on motor functions. J. Biol. Chem. 274, 37840-37844 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 37840-37844
    • Sasaki, N.1    Asukagawa, H.2    Yasuda, R.3    Hiratsuka, T.4    Sutoh, K.5
  • 24
    • 0028075752 scopus 로고
    • How molecular motors work
    • Spudich, J. A. How molecular motors work. Nature 372, 515-518 (1994).
    • (1994) Nature , vol.372 , pp. 515-518
    • Spudich, J.A.1
  • 25
    • 0035793563 scopus 로고    scopus 로고
    • Two conserved lysines at the 50/20-kDa junction of myosin are necessary for triggering actin activation
    • Joel, P. B., Trybus, K. M. & Sweeney, H. L. Two conserved lysines at the 50/20-kDa junction of myosin are necessary for triggering actin activation. J. Biol. Chem. 276, 2998-3003 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 2998-3003
    • Joel, P.B.1    Trybus, K.M.2    Sweeney, H.L.3
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-325 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-325
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 28
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 30
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.