메뉴 건너뛰기




Volumn 329, Issue 5, 2003, Pages 963-972

Refined model of the 10 S conformation of smooth muscle myosin by cryo-electron microscopy 3D image reconstruction

Author keywords

2D crystalline arrays; Lipid monolayer; Myosin light chains; Myosin regulation; Phosphorylation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; MYOSIN; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN; LIPID;

EID: 0038545279     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00516-3     Document Type: Article
Times cited : (79)

References (52)
  • 1
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves M.A., Holmes K.C. Structural mechanism of muscle contraction. Annu. Rev. Biochem. 68:1999;687-728.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 3
    • 0025825087 scopus 로고
    • Regulation of cytoplasmic and smooth muscle myosin
    • Sellers J.R. Regulation of cytoplasmic and smooth muscle myosin. Curr. Opin. Cell Biol. 3:1991;98-104.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 98-104
    • Sellers, J.R.1
  • 4
    • 0025752350 scopus 로고
    • Assembly of cytoplasmic and smooth muscle myosin
    • Trybus K.M. Assembly of cytoplasmic and smooth muscle myosin. Curr. Opin. Cell Biol. 3:1991;105-111.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 105-111
    • Trybus, K.M.1
  • 5
    • 0028918058 scopus 로고
    • Two heads are required for phosphorylation-dependent regulation of smooth muscle myosin
    • Cremo C.R., Sellers J.R., Facemyer K.C. Two heads are required for phosphorylation-dependent regulation of smooth muscle myosin. J. Biol. Chem. 270:1995;2171-2175.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2171-2175
    • Cremo, C.R.1    Sellers, J.R.2    Facemyer, K.C.3
  • 6
    • 0032561361 scopus 로고    scopus 로고
    • A long, weakly charged actin-binding loop is required for phosphorylation-dependent regulation of smooth muscle myosin
    • Rovner A.S. A long, weakly charged actin-binding loop is required for phosphorylation-dependent regulation of smooth muscle myosin. J. Biol. Chem. 273:1998;27939-27944.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27939-27944
    • Rovner, A.S.1
  • 7
    • 0032540958 scopus 로고    scopus 로고
    • The light chain-binding domain of the smooth muscle myosin heavy chain is not the only determinant of regulation
    • Trybus K.M., Naroditskaya V., Sweeney H.L. The light chain-binding domain of the smooth muscle myosin heavy chain is not the only determinant of regulation. J. Biol. Chem. 273:1998;18423-18428.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18423-18428
    • Trybus, K.M.1    Naroditskaya, V.2    Sweeney, H.L.3
  • 9
    • 0035836733 scopus 로고    scopus 로고
    • Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2
    • Wendt T., Taylor D., Trybus K.M., Taylor K. Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2. Proc. Natl Acad. Sci. USA. 98:2001;4361-4366.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4361-4366
    • Wendt, T.1    Taylor, D.2    Trybus, K.M.3    Taylor, K.4
  • 10
    • 0033611141 scopus 로고    scopus 로고
    • Visualization of head-head interactions in the inhibited state of smooth muscle myosin
    • Wendt T., Taylor D., Messier T., Trybus K.M., Taylor K.A. Visualization of head-head interactions in the inhibited state of smooth muscle myosin. J. Cell. Biol. 147:1999;1385-1390.
    • (1999) J. Cell. Biol. , vol.147 , pp. 1385-1390
    • Wendt, T.1    Taylor, D.2    Messier, T.3    Trybus, K.M.4    Taylor, K.A.5
  • 11
    • 0022371434 scopus 로고
    • Mechanism of the phosphorylation-dependent regulation of smooth muscle heavy meromyosin
    • Sellers J. Mechanism of the phosphorylation-dependent regulation of smooth muscle heavy meromyosin. J. Biol. Chem. 260:1985;15815-15819.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15815-15819
    • Sellers, J.1
  • 12
    • 0020678721 scopus 로고
    • Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules
    • Craig R., Smith R., Kendrick-Jones J. Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules. Nature. 302:1983;436-439.
    • (1983) Nature , vol.302 , pp. 436-439
    • Craig, R.1    Smith, R.2    Kendrick-Jones, J.3
  • 13
    • 0020181786 scopus 로고
    • Electron microscopic studies of myosin molecules from chicken gizzard muscle I: The formation of the intramolecular loop in the myosin tail
    • Onishi H., Wakabayashi T. Electron microscopic studies of myosin molecules from chicken gizzard muscle I: the formation of the intramolecular loop in the myosin tail. J. Biochem. (Tokyo). 92:1982;871-879.
    • (1982) J. Biochem. (Tokyo) , vol.92 , pp. 871-879
    • Onishi, H.1    Wakabayashi, T.2
  • 14
    • 0020451509 scopus 로고
    • A bent monomeric conformation of myosin from smooth muscle
    • Trybus K.M., Huiatt T.W., Lowey S. A bent monomeric conformation of myosin from smooth muscle. Proc. Natl Acad. Sci. USA. 79:1982;6151-6155.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 6151-6155
    • Trybus, K.M.1    Huiatt, T.W.2    Lowey, S.3
  • 15
    • 0023461924 scopus 로고
    • Conformational changes in myosin and heavy meromyosin from chicken gizzard associated with phosphorylation
    • Nag S., Suzuki H., Sosinski J., Seidel J.C. Conformational changes in myosin and heavy meromyosin from chicken gizzard associated with phosphorylation. Prog. Clin. Biol. Res. 245:1987;91-108.
    • (1987) Prog. Clin. Biol. Res. , vol.245 , pp. 91-108
    • Nag, S.1    Suzuki, H.2    Sosinski, J.3    Seidel, J.C.4
  • 16
    • 0026035307 scopus 로고
    • A folded (10 S) conformer of myosin from a striated muscle and its implications for regulation of ATPase activity
    • Ankrett R.J., Rowe A.J., Cross R.A., Kendrick-Jones J., Bagshaw C.R. A folded (10 S) conformer of myosin from a striated muscle and its implications for regulation of ATPase activity. J. Mol. Biol. 217:1991;323-335.
    • (1991) J. Mol. Biol. , vol.217 , pp. 323-335
    • Ankrett, R.J.1    Rowe, A.J.2    Cross, R.A.3    Kendrick-Jones, J.4    Bagshaw, C.R.5
  • 19
    • 0027474019 scopus 로고
    • Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers
    • Taylor K.A., Taylor D.W. Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers. J. Mol. Biol. 230:1993;196-205.
    • (1993) J. Mol. Biol. , vol.230 , pp. 196-205
    • Taylor, K.A.1    Taylor, D.W.2
  • 20
    • 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. 94:1998;559-571.
    • (1998) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 22
    • 0027419741 scopus 로고
    • Chimeric regulatory light chains as probes of smooth muscle myosin function
    • Trybus K.M., Chatman T.A. Chimeric regulatory light chains as probes of smooth muscle myosin function. J. Biol. Chem. 268:1993;4412-4419.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4412-4419
    • Trybus, K.M.1    Chatman, T.A.2
  • 23
    • 0029643912 scopus 로고    scopus 로고
    • Structure of the regulatory domain of scallop myosin at 2 Å resolution: Implications for regulation
    • Houdusse A., Cohen C. Structure of the regulatory domain of scallop myosin at 2 Å resolution: implications for regulation. Structure. 4:1996;21-32.
    • (1996) Structure , vol.4 , pp. 21-32
    • Houdusse, A.1    Cohen, C.2
  • 25
    • 0034104605 scopus 로고    scopus 로고
    • The interaction between the regulatory light chain domains on two heads is critical for regulation of smooth muscle myosin
    • Li X.D., Saito J., Ikebe R., Mabuchi K., Ikebe M. The interaction between the regulatory light chain domains on two heads is critical for regulation of smooth muscle myosin. Biochemistry. 39:2000;2254-2260.
    • (2000) Biochemistry , vol.39 , pp. 2254-2260
    • Li, X.D.1    Saito, J.2    Ikebe, R.3    Mabuchi, K.4    Ikebe, M.5
  • 26
    • 0035051492 scopus 로고    scopus 로고
    • Two new modes of smooth muscle myosin regulation by the interaction between the two regulatory light chains, and by the S2 domain
    • Konishi K., Kojima S., Katoh T., Yazawa M., Kato K., Fujiwara K., Onishi H. Two new modes of smooth muscle myosin regulation by the interaction between the two regulatory light chains, and by the S2 domain. J. Biochem. (Tokyo). 129:2001;365-372.
    • (2001) J. Biochem. (Tokyo) , vol.129 , pp. 365-372
    • Konishi, K.1    Kojima, S.2    Katoh, T.3    Yazawa, M.4    Kato, K.5    Fujiwara, K.6    Onishi, H.7
  • 27
    • 0033575291 scopus 로고    scopus 로고
    • Phosphorylation-dependent structural changes in the regulatory light chain domain of smooth muscle heavy meromyosin
    • Wu X., Clack B.A., Zhi G., Stull J.T., Cremo C.R. Phosphorylation-dependent structural changes in the regulatory light chain domain of smooth muscle heavy meromyosin. J. Biol. Chem. 274:1999;20328-20335.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20328-20335
    • Wu, X.1    Clack, B.A.2    Zhi, G.3    Stull, J.T.4    Cremo, C.R.5
  • 29
    • 0034623233 scopus 로고    scopus 로고
    • Funtional consequences of mutations in the smooth muscle myosin heavy chain at sites implicated in familial hypertrophic cardiomyopathy
    • Yamashita H., Tyska M.J., Warshaw D.M., Lowey S., Trybus K.M. Funtional consequences of mutations in the smooth muscle myosin heavy chain at sites implicated in familial hypertrophic cardiomyopathy. J. Biol. Chem. 275:2000;28045-28052.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28045-28052
    • Yamashita, H.1    Tyska, M.J.2    Warshaw, D.M.3    Lowey, S.4    Trybus, K.M.5
  • 30
    • 0036421146 scopus 로고    scopus 로고
    • Molecular modeling of averaged rigor crossbridges from tomograms of insect flight muscle: A range of strongly-bound structures for the late-stage power stroke
    • Chen L.F., Winkler H., Reedy M.K., Reedy M.C., Taylor K.A. Molecular modeling of averaged rigor crossbridges from tomograms of insect flight muscle: a range of strongly-bound structures for the late-stage power stroke. J. Struct. Biol. 138:2002;92-104.
    • (2002) J. Struct. Biol. , vol.138 , pp. 92-104
    • Chen, L.F.1    Winkler, H.2    Reedy, M.K.3    Reedy, M.C.4    Taylor, K.A.5
  • 31
    • 0035968217 scopus 로고    scopus 로고
    • ADP binding induces an asymmetry between the heads of unphosphorylated myosin
    • Berger C.E., Fagnant P.M., Heizmann S., Trybus K.M., Geeves M.A. ADP binding induces an asymmetry between the heads of unphosphorylated myosin. J. Biol. Chem. 276:2001;23240-23245.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23240-23245
    • Berger, C.E.1    Fagnant, P.M.2    Heizmann, S.3    Trybus, K.M.4    Geeves, M.A.5
  • 32
    • 0034731348 scopus 로고    scopus 로고
    • Regulation of asymmetric smooth muscle myosin II molecules
    • Sweeney H.L., Chen L.Q., Trybus K.M. Regulation of asymmetric smooth muscle myosin II molecules. J. Biol. Chem. 275:2000;41273-41277.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41273-41277
    • Sweeney, H.L.1    Chen, L.Q.2    Trybus, K.M.3
  • 33
    • 0035798653 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation is absent in a nonmuscle heavy meromyosin construct with one complete head and one head lacking the motor domain
    • Cremo C.R., Wang F., Facemyer K., Sellers J.R. Phosphorylation-dependent regulation is absent in a nonmuscle heavy meromyosin construct with one complete head and one head lacking the motor domain. J. Biol. Chem. 276:2001;41465-41472.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41465-41472
    • Cremo, C.R.1    Wang, F.2    Facemyer, K.3    Sellers, J.R.4
  • 37
    • 0027300234 scopus 로고
    • Myosin light chain phosphorylation in vertebrate striated muscle: Regulation and function
    • Sweeney H.L., Bowman B.F., Stull J.T. Myosin light chain phosphorylation in vertebrate striated muscle: regulation and function. Am. J. Physiol. 264:1993;C1085-C1095.
    • (1993) Am. J. Physiol. , vol.264
    • Sweeney, H.L.1    Bowman, B.F.2    Stull, J.T.3
  • 38
    • 0022270772 scopus 로고
    • 2+ on the conformation and enzymatic activity of smooth muscle myosin
    • 2+ on the conformation and enzymatic activity of smooth muscle myosin. J. Biol. Chem. 260:1985;13146-13153.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13146-13153
    • Ikebe, M.1    Hartshorne, D.J.2
  • 39
    • 0026506363 scopus 로고
    • Formation of 2D paracrystals of F-actin on phospholipid layers mixed with quaternary ammonium surfactants
    • Taylor K.A., Taylor D.W. Formation of 2D paracrystals of F-actin on phospholipid layers mixed with quaternary ammonium surfactants. J. Struct. Biol. 108:1992;140-147.
    • (1992) J. Struct. Biol. , vol.108 , pp. 140-147
    • Taylor, K.A.1    Taylor, D.W.2
  • 40
    • 0013823053 scopus 로고
    • A new method of preparation of a self-perforated micro plastic grid and its application
    • Fukami A., Adachi K. A new method of preparation of a self-perforated micro plastic grid and its application. J. Electron Microsc. 14:1965;112-118.
    • (1965) J. Electron Microsc. , vol.14 , pp. 112-118
    • Fukami, A.1    Adachi, K.2
  • 41
    • 0027554794 scopus 로고
    • SPECTRA: A system for processing electron images of crystals
    • Schmid M., Dargahi R., Tam M. SPECTRA: a system for processing electron images of crystals. Ultramicroscopy. 48:1993;251-264.
    • (1993) Ultramicroscopy , vol.48 , pp. 251-264
    • Schmid, M.1    Dargahi, R.2    Tam, M.3
  • 42
    • 0029928874 scopus 로고    scopus 로고
    • CTF determination of images of ice-embedded single particles using a graphics interface
    • Zhou Z.H., Hardt S., Wang B., Sherman M.B., Jakana J., Chiu W. CTF determination of images of ice-embedded single particles using a graphics interface. J. Struct. Biol. 116:1996;216-222.
    • (1996) J. Struct. Biol. , vol.116 , pp. 216-222
    • Zhou, Z.H.1    Hardt, S.2    Wang, B.3    Sherman, M.B.4    Jakana, J.5    Chiu, W.6
  • 43
    • 0029670614 scopus 로고    scopus 로고
    • Visualization of β-sheets and side-chain clusters in two-dimensional periodic arrays of streptavidin on phospholipid monolayers by electron crystallography
    • Avila-Sakar A.J., Chiu W. Visualization of β-sheets and side-chain clusters in two-dimensional periodic arrays of streptavidin on phospholipid monolayers by electron crystallography. Biophys. J. 70:1996;57-68.
    • (1996) Biophys. J. , vol.70 , pp. 57-68
    • Avila-Sakar, A.J.1    Chiu, W.2
  • 45
    • 0020018227 scopus 로고
    • Three-dimensional structure determination by electron microscopy of two-dimensional crystals
    • Amos L.A., Henderson R., Unwin P.N.T. Three-dimensional structure determination by electron microscopy of two-dimensional crystals. Prog. Biophys. Mol. Biol. 39:1982;183-231.
    • (1982) Prog. Biophys. Mol. Biol. , vol.39 , pp. 183-231
    • Amos, L.A.1    Henderson, R.2    Unwin, P.N.T.3
  • 46
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Project C.C. The CCP4 Suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
    • Project, C.C.1
  • 47
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis. 18:1997;2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 48
    • 0028978047 scopus 로고
    • Computer modelling of the α-helical coiled coil: Packing of side-chains in the inner core
    • Offer G., Sessions R. Computer modelling of the α-helical coiled coil: packing of side-chains in the inner core. J. Mol. Biol. 249:1995;967-987.
    • (1995) J. Mol. Biol. , vol.249 , pp. 967-987
    • Offer, G.1    Sessions, R.2
  • 49
    • 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 Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 50
    • 0001832403 scopus 로고
    • Restrained real-space macromolecular atomic refinement using a new resolution-dependent electron-density function
    • Chapman M.S. Restrained real-space macromolecular atomic refinement using a new resolution-dependent electron-density function. Acta Crystallog. sect. A. 51:1995;69-80.
    • (1995) Acta Crystallog. sect. A , vol.51 , pp. 69-80
    • Chapman, M.S.1
  • 51
    • 84913050729 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud D.E., Ten Eyck L.F., Mathews B.W. An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallog. sect. A. 43:1987;489-501.
    • (1987) Acta Crystallog. sect. A , vol.43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Mathews, B.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.