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Volumn 105, Issue 35, 2008, Pages 12867-12872

Actin-binding cleft closure in myosin II probed by site-directed spin labeling and pulsed EPR

Author keywords

Actomyosin; Dipolar interaction; Double electron electron resonance

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; MYOSIN; MYOSIN 2; MYOSIN ADENOSINE TRIPHOSPHATASE; NUCLEOTIDE; UNCLASSIFIED DRUG; VANADIC ACID;

EID: 51349133261     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0802286105     Document Type: Article
Times cited : (42)

References (44)
  • 1
    • 0032005265 scopus 로고    scopus 로고
    • Myosins: Matching functions with motors
    • Baker JP, Titus MA (1998) Myosins: Matching functions with motors. Curr Opin Cell Biol 10:80-86.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 80-86
    • Baker, J.P.1    Titus, M.A.2
  • 2
    • 0042019998 scopus 로고    scopus 로고
    • Dictyostelium myosin II as a model to study the actin-myosin interactions during force generation
    • Sasaki N, Ohkura R, Sutoh K (2002) Dictyostelium myosin II as a model to study the actin-myosin interactions during force generation. J Muscle Res Cell Motil 23:697-702.
    • (2002) J Muscle Res Cell Motil , vol.23 , pp. 697-702
    • Sasaki, N.1    Ohkura, R.2    Sutoh, K.3
  • 3
    • 0027767689 scopus 로고
    • A functional recombinant myosin II lacking a regulatory light chain-binding site
    • Uyeda TQ, Spudich JA (1993) A functional recombinant myosin II lacking a regulatory light chain-binding site. Science 262:1867-1870.
    • (1993) Science , vol.262 , pp. 1867-1870
    • Uyeda, T.Q.1    Spudich, J.A.2
  • 4
    • 0027194702 scopus 로고
    • Three-dimensional structure of myosin subfragment-1: A molecular motor
    • Rayment I, et al. (1993) Three-dimensional structure of myosin subfragment-1: A molecular motor. Science 261:50-58.
    • (1993) Science , vol.261 , pp. 50-58
    • Rayment, I.1
  • 5
    • 0034624066 scopus 로고    scopus 로고
    • X-ray structures of the apo and MgATP-bound states of Dictyostelium discoideum myosin motor domain
    • Bauer CB, Holden HM, Thoden JB, Smith R, Rayment I (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
  • 6
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesium(II). ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution
    • Smith CA, Rayment I (1996) X-ray structure of the magnesium(II). ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution. Biochemistry 35:5404-5417.
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 7
    • 10644225267 scopus 로고    scopus 로고
    • Three myosin V structures delineate essential features of chemo-mechanical transduction
    • Coureux PD, Sweeney HL, Houdusse A (2004) Three myosin V structures delineate essential features of chemo-mechanical transduction. EMBO J 23:4527-4537.
    • (2004) EMBO J , vol.23 , pp. 4527-4537
    • Coureux, P.D.1    Sweeney, H.L.2    Houdusse, A.3
  • 8
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment I, et al. (1993) Structure of the actin-myosin complex and its implications for muscle contraction. Science 261:58-65.
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1
  • 9
    • 0030768794 scopus 로고    scopus 로고
    • X-ray structures of the MgADP, MgATPgammaS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain
    • Gulick AM, Bauer CB, Thoden JB, Rayment I (1997) X-ray structures of the MgADP, MgATPgammaS, 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
  • 10
    • 0011364439 scopus 로고    scopus 로고
    • Fisher AJ, et al. (1995) Structural studies of myosin:nucleotide complexes: A revised model for the molecular basis of muscle contraction. Biophys J 68:19S-26S, and discussion (1995) 68:27S-28S.
    • Fisher AJ, et al. (1995) Structural studies of myosin:nucleotide complexes: A revised model for the molecular basis of muscle contraction. Biophys J 68:19S-26S, and discussion (1995) 68:27S-28S.
  • 11
    • 0029159959 scopus 로고
    • X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4
    • Fisher AJ, et al. (1995) X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4. Biochemistry 34:8960-8972.
    • (1995) Biochemistry , vol.34 , pp. 8960-8972
    • Fisher, A.J.1
  • 12
    • 0141843643 scopus 로고    scopus 로고
    • Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide
    • Holmes KC, Angert I, Kull FJ, Jahn W, Schröder RR (2003) Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide. Nature 425:423-427.
    • (2003) Nature , vol.425 , pp. 423-427
    • Holmes, K.C.1    Angert, I.2    Kull, F.J.3    Jahn, W.4    Schröder, R.R.5
  • 13
    • 0141732282 scopus 로고    scopus 로고
    • A structural state of the myosin V motor without bound nucleotide
    • Coureux PD, et al. (2003) A structural state of the myosin V motor without bound nucleotide. Nature 425:419-423.
    • (2003) Nature , vol.425 , pp. 419-423
    • Coureux, P.D.1
  • 15
    • 34247875370 scopus 로고    scopus 로고
    • Rigor-like structures from muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor
    • Yang Y, et al. (2007) Rigor-like structures from muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor. Structure 15:553-564.
    • (2007) Structure , vol.15 , pp. 553-564
    • Yang, Y.1
  • 17
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • Hubbell WL, Altenbach C, Hubbell CM, Khorana HG (2003) Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. Adv Protein Chem 63:243-290.
    • (2003) Adv Protein Chem , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 18
    • 33749041288 scopus 로고    scopus 로고
    • Recent advances and applications of site-directed spin labeling
    • Fanucci GE, Cafiso DS (2006) Recent advances and applications of site-directed spin labeling. Curr Opin Struct Biol 16:644-653.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 644-653
    • Fanucci, G.E.1    Cafiso, D.S.2
  • 19
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • Rabenstein MD, Shin YK (1995) Determination of the distance between two spin labels attached to a macromolecule. Proc Natl Acad Sci USA 92:8239-8243.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 21
    • 0036789728 scopus 로고    scopus 로고
    • Molecular dynamics simulation of site-directed spin labeling: Experimental validation in muscle fibers
    • LaConte LE, Voelz V, Nelson W, Enz M, Thomas DD (2002) Molecular dynamics simulation of site-directed spin labeling: Experimental validation in muscle fibers. Biophys J 83:1854-1866.
    • (2002) Biophys J , vol.83 , pp. 1854-1866
    • LaConte, L.E.1    Voelz, V.2    Nelson, W.3    Enz, M.4    Thomas, D.D.5
  • 22
    • 21644446664 scopus 로고    scopus 로고
    • Explicit treatment of spin labels in modeling of distance constraints from dipolar EPR and DEER
    • Sale K, Song L, Liu YS, Perozo E, Fajer P (2005) Explicit treatment of spin labels in modeling of distance constraints from dipolar EPR and DEER. J Am Chem Soc 127:9334-9335.
    • (2005) J Am Chem Soc , vol.127 , pp. 9334-9335
    • Sale, K.1    Song, L.2    Liu, Y.S.3    Perozo, E.4    Fajer, P.5
  • 23
    • 32044470052 scopus 로고    scopus 로고
    • Structural dynamics of the actin-myosin interface by site-directed spectroscopy
    • Korman VL, Anderson SE, Prochniewicz E, Titus MA, Thomas DD (2006) Structural dynamics of the actin-myosin interface by site-directed spectroscopy. J Mol Biol 356:1107-1117.
    • (2006) J Mol Biol , vol.356 , pp. 1107-1117
    • Korman, V.L.1    Anderson, S.E.2    Prochniewicz, E.3    Titus, M.A.4    Thomas, D.D.5
  • 24
    • 33646595393 scopus 로고    scopus 로고
    • Toward understanding actin activation of myosin ATPase: The role of myosin surface loops
    • Onishi H, Mikhailenko SV, Morales MF (2006) Toward understanding actin activation of myosin ATPase: The role of myosin surface loops. Proc Natl Acad Sci USA 103:6136-6141.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6136-6141
    • Onishi, H.1    Mikhailenko, S.V.2    Morales, M.F.3
  • 25
    • 34547676382 scopus 로고    scopus 로고
    • Myosin cleft closure by double electron-electron resonance and dipolar EPR
    • Fajer PG, et al. (2007) Myosin cleft closure by double electron-electron resonance and dipolar EPR. J Phys Condens Matter 19:285208.
    • (2007) J Phys Condens Matter , vol.19 , pp. 285208
    • Fajer, P.G.1
  • 27
    • 24144502337 scopus 로고    scopus 로고
    • Accessibility of nitroxide side chains: Absolute Heisenberg exchange rates from power saturation EPR
    • Altenbach C, Froncisz W, Hemker R, McHaourab H, Hubbell WL (2005) Accessibility of nitroxide side chains: Absolute Heisenberg exchange rates from power saturation EPR. Biophys J 89:2103-2112.
    • (2005) Biophys J , vol.89 , pp. 2103-2112
    • Altenbach, C.1    Froncisz, W.2    Hemker, R.3    McHaourab, H.4    Hubbell, W.L.5
  • 28
    • 40949163372 scopus 로고    scopus 로고
    • Distance measurements in the borderline region of applicability of CW EPR and DEER: A model study on a homologous series of spin-labelled peptides
    • Banham JE, et al. (2008) Distance measurements in the borderline region of applicability of CW EPR and DEER: A model study on a homologous series of spin-labelled peptides. J Magn Reson 191:202-218.
    • (2008) J Magn Reson , vol.191 , pp. 202-218
    • Banham, J.E.1
  • 29
    • 1542286175 scopus 로고    scopus 로고
    • A new structural state of myosin
    • Kull FJ, Endow SA (2004) A new structural state of myosin. Trends Biochem Sci 29:103-106.
    • (2004) Trends Biochem Sci , vol.29 , pp. 103-106
    • Kull, F.J.1    Endow, S.A.2
  • 31
    • 36148983388 scopus 로고    scopus 로고
    • Mapping electron paramagnetic resonance spin label conformations by the simulated scaling method
    • Fajer MI, Li H, Yang W, Fajer PG (2007) Mapping electron paramagnetic resonance spin label conformations by the simulated scaling method. J Am Chem Soc 129:13840-13846.
    • (2007) J Am Chem Soc , vol.129 , pp. 13840-13846
    • Fajer, M.I.1    Li, H.2    Yang, W.3    Fajer, P.G.4
  • 32
    • 33846061625 scopus 로고    scopus 로고
    • Dynamics of the nucleotide pocket of myosin measured by spin-labeled nucleotides
    • Naber N, Purcell TJ, Pate E, Cooke R (2007) Dynamics of the nucleotide pocket of myosin measured by spin-labeled nucleotides. Biophys J 92:172-184.
    • (2007) Biophys J , vol.92 , pp. 172-184
    • Naber, N.1    Purcell, T.J.2    Pate, E.3    Cooke, R.4
  • 33
    • 46749142507 scopus 로고    scopus 로고
    • Structure and dynamics of the force generating domain of myosin probed by site-directed spin labeling and multifrequency electron paramagnetic resonance
    • Nesmelov YE, Agafonov RV, Burr A, Weber RT, Thomas DD (2008) Structure and dynamics of the force generating domain of myosin probed by site-directed spin labeling and multifrequency electron paramagnetic resonance. Biophys J 95:247-256.
    • (2008) Biophys J , vol.95 , pp. 247-256
    • Nesmelov, Y.E.1    Agafonov, R.V.2    Burr, A.3    Weber, R.T.4    Thomas, D.D.5
  • 34
    • 51649127767 scopus 로고    scopus 로고
    • Muscle and nonmuscle myosins probed by a spin label at equivalent sites in the force-generating domain
    • in press
    • Agafonov RV, Titus MA, Nesmelov YE, Thomas DD (2008) Muscle and nonmuscle myosins probed by a spin label at equivalent sites in the force-generating domain. Proc Natl Acad Sci USA, in press.
    • (2008) Proc Natl Acad Sci USA
    • Agafonov, R.V.1    Titus, M.A.2    Nesmelov, Y.E.3    Thomas, D.D.4
  • 35
    • 0030564835 scopus 로고    scopus 로고
    • Cooperativity in F-actin: Binding of gelsolin at the barbed end affects structure and dynamics of the whole filament
    • Prochniewicz E, Zhang Q, Janmey PA, Thomas DD (1996) Cooperativity in F-actin: binding of gelsolin at the barbed end affects structure and dynamics of the whole filament. J Mol Biol 260:756-766.
    • (1996) J Mol Biol , vol.260 , pp. 756-766
    • Prochniewicz, E.1    Zhang, Q.2    Janmey, P.A.3    Thomas, D.D.4
  • 36
    • 0025346254 scopus 로고
    • Transmembrane protein structure: Spin labeling of bacteriorhodopsin mutants
    • Altenbach C, Marti T, Khorana HG, Hubbell WL (1990) Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants. Science 248:1088-1092.
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 37
    • 2442553272 scopus 로고    scopus 로고
    • Electron paramagnetic resonance reveals a large-scale conformational change in the cytoplasmic domain of phospholamban upon binding to the sarcoplasmic reticulum Ca-ATPase
    • Kirby TL, Karim CB, Thomas DD (2004) Electron paramagnetic resonance reveals a large-scale conformational change in the cytoplasmic domain of phospholamban upon binding to the sarcoplasmic reticulum Ca-ATPase. Biochemistry 43:5842-5852.
    • (2004) Biochemistry , vol.43 , pp. 5842-5852
    • Kirby, T.L.1    Karim, C.B.2    Thomas, D.D.3
  • 38
    • 37049032797 scopus 로고    scopus 로고
    • A paramagnetic molecular voltmeter
    • Surek JT, Thomas DD (2008) A paramagnetic molecular voltmeter. J Magn Reson 190:7-25.
    • (2008) J Magn Reson , vol.190 , pp. 7-25
    • Surek, J.T.1    Thomas, D.D.2
  • 39
    • 0000326938 scopus 로고    scopus 로고
    • Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm
    • Budil DE, Lee S, Saxena S, Freed JH (1996) Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm. J Magn Reson A 120:155-189.
    • (1996) J Magn Reson A , vol.120 , pp. 155-189
    • Budil, D.E.1    Lee, S.2    Saxena, S.3    Freed, J.H.4
  • 40
    • 0036290220 scopus 로고    scopus 로고
    • Direct conversion of EPR dipolar time evolution data to distance distributions
    • Jeschke G, Koch A, Jonas U, Godt A (2002) Direct conversion of EPR dipolar time evolution data to distance distributions. J Magn Reson 155:72-82.
    • (2002) J Magn Reson , vol.155 , pp. 72-82
    • Jeschke, G.1    Koch, A.2    Jonas, U.3    Godt, A.4
  • 41
    • 0037112592 scopus 로고    scopus 로고
    • Distance measurements in the nanometer range by pulse EPR
    • Jeschke G (2002) Distance measurements in the nanometer range by pulse EPR. Chemphyschem 3:927-932.
    • (2002) Chemphyschem , vol.3 , pp. 927-932
    • Jeschke, G.1
  • 43
    • 0029878720 scopus 로고    scopus 로고
    • Humphrey W, Dalke A, Schulten K (1996) VMD: Visual molecular dynamics. J Mol Graphics 14, 33-38.
    • Humphrey W, Dalke A, Schulten K (1996) VMD: Visual molecular dynamics. J Mol Graphics 14, 33-38.
  • 44
    • 0035983171 scopus 로고    scopus 로고
    • Structural determination of spin label immobilization and orientation: A Monte Carlo minimization approach
    • Sale K, Sar C, Sharp KA, Hideg K, Fajer PG (2002) Structural determination of spin label immobilization and orientation: A Monte Carlo minimization approach. J Magn Reson 156:104-112.
    • (2002) J Magn Reson , vol.156 , pp. 104-112
    • Sale, K.1    Sar, C.2    Sharp, K.A.3    Hideg, K.4    Fajer, P.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.