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Volumn 159, Issue 6, 2002, Pages 983-991

The prepower stroke conformation of myosin V

Author keywords

Force; Mechanism; Thermal ratchet; Titling lever; Walking

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; APOENZYME; MYOSIN HEAVY CHAIN; MYOSIN V; PROTEIN SUBUNIT;

EID: 0037164812     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200208172     Document Type: Article
Times cited : (110)

References (51)
  • 1
    • 0034624066 scopus 로고    scopus 로고
    • X-ray structures of the apo and MgATP-bound states of Dictyostelium discoideum myosin motor domain
    • Bauer, C.B., H.M. Holden, J.B. Thoden, R. Smith, and I. Rayment. 2000. X-ray structures of the apo and MgATP-bound states of Dictyostelium discoideum myosin motor domain. J. Biol. Chem. 275:38494-38499.
    • (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
  • 3
    • 0030678623 scopus 로고    scopus 로고
    • Flexibility within myosin heads revealed by negative stain and single-particle analysis
    • Burgess, S.A., M. Walker, H.D. White, and J. Trinick. 1997. Flexibility within myosin heads revealed by negative stain and single-particle analysis. J. Cell Biol. 139:675-681.
    • (1997) J. Cell Biol. , vol.139 , pp. 675-681
    • Burgess, S.A.1    Walker, M.2    White, H.D.3    Trinick, J.4
  • 5
    • 0035943690 scopus 로고    scopus 로고
    • Kinetic mechanism and regulation of myosin VI
    • de la Cruz, E.M., E.M. Ostap, and H.L. Sweeney. 2001. Kinetic mechanism and regulation of myosin VI. J. Biol. Chem. 276:32373-32381.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32373-32381
    • De la Cruz, E.M.1    Ostap, E.M.2    Sweeney, H.L.3
  • 6
    • 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., Y. Freyzon, K.M. Trybus, and C. Cohen. 1998. 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) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 7
    • 0027068050 scopus 로고
    • Primary structure and cellular-localization of chicken brain myosin-V P190, an unconventional myosin with calmodulin light-chains
    • Espreafico, E.M., R.E. Cheney, M. Matteoli, A.A.C. Nascimento, P.V. Decamilli, R.E. Larson, and M.S. Mooseker. 1992. Primary structure and cellular-localization of chicken brain myosin-V P190, an unconventional myosin with calmodulin light-chains. J. Cell Biol. 119:1541-1557.
    • (1992) J. Cell Biol. , vol.119 , pp. 1541-1557
    • Espreafico, E.M.1    Cheney, R.E.2    Matteoli, M.3    Nascimento, A.A.C.4    Decamilli, P.V.5    Larson, R.E.6    Mooseker, M.S.7
  • 10
    • 0029975088 scopus 로고    scopus 로고
    • Spider and web-processing and visualization of images in 3D electronmicroscopy and related fields
    • Frank, J., M. Radermacher, P. Penczek, J. Zhu, Y.H. Li, M. Ladjadj, and A. Leith. 1996. Spider and web-processing and visualization of images in 3D electronmicroscopy and related fields. J. Struct. Biol. 116:190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.H.5    Ladjadj, M.6    Leith, A.7
  • 11
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves, M.A., and K.C. Holmes. 1999. Structural mechanism of muscle contraction. Annu. Rev. Biochem. 68:687-728.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 12
    • 0033520114 scopus 로고    scopus 로고
    • Phosphorylation regulates the ADP-induced rotation of the light chain domain of smooth muscle myosin
    • Gollub, J., C.R. Cremo, and R. Cooke. 1999. Phosphorylation regulates the ADP-induced rotation of the light chain domain of smooth muscle myosin. Biochemistry. 38:10107-10118.
    • (1999) Biochemistry , vol.38 , pp. 10107-10118
    • Gollub, J.1    Cremo, C.R.2    Cooke, R.3
  • 13
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and M.C. Peitsch. 1997. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis. 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 14
    • 0030768794 scopus 로고    scopus 로고
    • X-ray structures of the MgADP, MgATP gamma S, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain
    • Gulick, A.M., C.B. Bauer, J.B. Thoden, and I. Rayment. 1997. X-ray structures of the MgADP, MgATP gamma S, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain. Biochemistry. 36:11619-11628.
    • (1997) Biochemistry , vol.36 , pp. 11619-11628
    • Gulick, A.M.1    Bauer, C.B.2    Thoden, J.B.3    Rayment, I.4
  • 15
    • 0029643912 scopus 로고    scopus 로고
    • Structure of the regulatory domain of scallop myosin at 2-angstrom resolution: Implications for regulation
    • Houdusse, A., and C. Cohen. 1996. Structure of the regulatory domain of scallop myosin at 2-angstrom resolution: Implications for regulation. Structure. 4:21-32.
    • (1996) Structure , vol.4 , pp. 21-32
    • Houdusse, A.1    Cohen, C.2
  • 16
    • 1642340974 scopus 로고    scopus 로고
    • Atomic structure of scallop myosin subfragment S1 complexed with MgADP: A novel conformation of the myosin head
    • Houdusse, A., V.N. Kalbokis, D. Himmel, A.G. Szent-Györgyi, and C. Cohen. 1999. Atomic structure of scallop myosin subfragment S1 complexed with MgADP: A novel conformation of the myosin head. Cell. 97:459-470.
    • (1999) Cell , vol.97 , pp. 459-470
    • Houdusse, A.1    Kalbokis, V.N.2    Himmel, D.3    Szent-Györgyi, A.G.4    Cohen, C.5
  • 17
    • 0035312384 scopus 로고    scopus 로고
    • Myosin motors: Missing structures and hidden springs
    • Houdusse, A., and H.L. Sweeney. 2001. Myosin motors: Missing structures and hidden springs. Curr. Opin. Struct. Biol. 11:182-194.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 182-194
    • Houdusse, A.1    Sweeney, H.L.2
  • 19
    • 0030773824 scopus 로고    scopus 로고
    • Molecular motors: Structural adaptations to cellular functions
    • Howard, J. 1997. Molecular motors: Structural adaptations to cellular functions. Nature. 389:561-567.
    • (1997) Nature , vol.389 , pp. 561-567
    • Howard, J.1
  • 20
    • 0014685163 scopus 로고
    • The mechanism of muscle contraction
    • Huxley, H.E. 1969. The mechanism of muscle contraction. Science. 164:1356-1366.
    • (1969) Science , vol.164 , pp. 1356-1366
    • Huxley, H.E.1
  • 21
    • 0029562245 scopus 로고
    • A 32-degree tail swing in brush-border myosin-I on ADP release
    • Jontes, J.D., E.M. Wilson-Kubalek, and R.A. Milligan. 1995. A 32-degree tail swing in brush-border myosin-I on ADP release. Nature. 378:751-753.
    • (1995) Nature , vol.378 , pp. 751-753
    • Jontes, J.D.1    Wilson-Kubalek, E.M.2    Milligan, R.A.3
  • 22
    • 0021717613 scopus 로고
    • Structure of the myosin projections on native thick filaments from vertebrate skeletal-muscle
    • Knight, P., and J. Trinick. 1984. Structure of the myosin projections on native thick filaments from vertebrate skeletal-muscle. J. Mol. Biol. 177:461-482.
    • (1984) J. Mol. Biol. , vol.177 , pp. 461-482
    • Knight, P.1    Trinick, J.2
  • 23
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz, M., D. Popp, and K.C. Holmes. 1993. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 24
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis ofacto-myosin
    • Lymn, R.W., and E.W. Taylor. 1971. Mechanism of adenosine triphosphate hydrolysis ofacto-myosin. Biochemistry. 10:4617-4624.
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 25
    • 0034719112 scopus 로고    scopus 로고
    • Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan W501 mutants: Implications for the open-closed transition identified by crystallography
    • Malnasi-Csizmadia, A., R.J. Woolley, and C.R. Bagshaw. 2000. Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan W501 mutants: Implications for the open-closed transition identified by crystallography. Biochemistry. 39:16135-16146.
    • (2000) Biochemistry , vol.39 , pp. 16135-16146
    • Malnasi-Csizmadia, A.1    Woolley, R.J.2    Bagshaw, C.R.3
  • 27
    • 0030832286 scopus 로고    scopus 로고
    • The structure of the acto-myosin subfragment 1 complex: Results of searches using data from electron microscopy and x-ray crystallography
    • Mendelson, R., and E.P. Morris. 1997. The structure of the acto-myosin subfragment 1 complex: Results of searches using data from electron microscopy and x-ray crystallography. Proc. Natl. Acad. Sci. USA. 94:8533-8538.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8533-8538
    • Mendelson, R.1    Morris, E.P.2
  • 28
    • 0035969240 scopus 로고    scopus 로고
    • Myosin V exhibits a high duty cycle and large unitary displacement
    • Moore, J.R., E.B. Krementsova, K.M. Trybus, and D.M. Warshaw. 2001. Myosin V exhibits a high duty cycle and large unitary displacement. J. Cell Biol. 155:625-635.
    • (2001) J. Cell Biol. , vol.155 , pp. 625-635
    • Moore, J.R.1    Krementsova, E.B.2    Trybus, K.M.3    Warshaw, D.M.4
  • 30
    • 0028393194 scopus 로고
    • The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryoelectron microscopy of biological particles
    • Penczek, P.A., R.A. Grassucci, and J. Frank. 1994. The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryoelectron microscopy of biological particles. Ultramicroscopy. 53:251-270.
    • (1994) Ultramicroscopy , vol.53 , pp. 251-270
    • Penczek, P.A.1    Grassucci, R.A.2    Frank, J.3
  • 34
    • 0035123582 scopus 로고    scopus 로고
    • Single-molecule tracking of myosins with genetically engineered amplifier domains
    • Ruff, C., M. Furch, B. Brenner, D.J. Manstein, and E. Meyhofer. 2001. Single-molecule tracking of myosins with genetically engineered amplifier domains. Nat. Struct. Biol. 8:226-229.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 226-229
    • Ruff, C.1    Furch, M.2    Brenner, B.3    Manstein, D.J.4    Meyhofer, E.5
  • 35
  • 37
    • 0034264852 scopus 로고    scopus 로고
    • A FRET-based sensor reveals large ATP hydrolysis-induced conformational changes and three distinct states of the molecular motor myosin
    • Shih, W.M., Z. Gryczynski, J.R. Lakowicz, and J.A. Spudich. 2000. A FRET-based sensor reveals large ATP hydrolysis-induced conformational changes and three distinct states of the molecular motor myosin. Cell. 102:683-694.
    • (2000) Cell , vol.102 , pp. 683-694
    • Shih, W.M.1    Gryczynski, Z.2    Lakowicz, J.R.3    Spudich, J.A.4
  • 38
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesiumII.ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Angstrom resolution
    • Smith, C.A., and I. Payment. 1996. X-ray structure of the magnesiumII.ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Angstrom resolution. Biochemistry. 35:5404-5417.
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Payment, I.2
  • 39
    • 0035881965 scopus 로고    scopus 로고
    • A fluorescence temperature-jump study of conformational transitions in myosin subfragment 1
    • Urbanke, C., and J. Wray. 2001. A fluorescence temperature-jump study of conformational transitions in myosin subfragment 1. Biochem. J. 358:165-173.
    • (2001) Biochem. J. , vol.358 , pp. 165-173
    • Urbanke, C.1    Wray, J.2
  • 40
    • 0029913456 scopus 로고    scopus 로고
    • The neck region of the myosin motor domain acts as a arm to generate movement
    • Uyeda, T.Q.P., P.D. Abramson, and J.A. Spudich. 1996. The neck region of the myosin motor domain acts as a arm to generate movement. Proc. Natl. Acad. Sci. USA. 93:4459-4464.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4459-4464
    • Uyeda, T.Q.P.1    Abramson, P.D.2    Spudich, J.A.3
  • 41
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale, R.D., and R.A. Milligan. 2000. The way things move: Looking under the hood of molecular motor proteins. Science. 288:88-95.
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 45
    • 0022419381 scopus 로고
    • Negative staining of myosin molecules
    • Walker, M., P. Knight, and J. Trinick. 1985. Negative staining of myosin molecules. J. Mol. Biol. 184:535-542.
    • (1985) J. Mol. Biol. , vol.184 , pp. 535-542
    • Walker, M.1    Knight, P.2    Trinick, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.