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

Volumn 94, Issue 5, 1998, Pages 559-571

  Dominguez, Roberto ^a,b   Freyzon, Yelena ^a,c   Trybus, Kathleen M ^a,d   Cohen, Carolyn ^a  

^a BRANDEIS UNIVERSITY   (United States)

^b BOSTON BIOMEDICAL RESEARCH INSTITUTE   (United States)

^c WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

^d UNIVERSITY OF VERMONT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN STRUCTURE; SMOOTH MUSCLE; VERTEBRATE;

VERTEBRATA;

EID: 0032483563     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81598-6     Document Type: Article

References (44)

1. Anson, M., Geeves, M.A., Kurzawa, S.E., and Manstein, D.J. (1996). Myosin motors with artificial lever arms. EMBO J. 15, 6069-6074.
2. Block, S.M. (1996). Fifty ways to love your lever: myosin motors. Cell 87, 151-157.
3. Brünger, A.T. (1992). X-PLOR, Version 3.1 Manual: A System for X-Ray Crystallography and NMR (New Haven, CT: Yale University Press).
4. Burghardt, T.P., Garamszegi, S.P., Park, S., and Ajtai, K. (1998). Tertiary structural changes in the cleft containing the ATP sensitive tryptophan and reactive thiol are consistent with pivoting of the myosin heavy chain at Gly699. Biochemistry 37, 8035-8047.
5. Cope, M.J.T., Whisstock, J., Rayment, I., and Kendrick-Jones, J. (1996). Conservation within the myosin motor domain: implications for structure and function. Structure 4, 969-987.
6. Cowtan, K.D. (1994). 'DM': an automated procedure for phase improvement by density modification. In Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography 31, 34-38.
7. Fisher, A.J., Smith, C.A., Thoden, J., Smith, R., Sutoh, K., Holden, H.M., and Rayment, I. (1995a). Structural studies of myosin:nucleotide complexes: a revised model for the molecular basis of muscle contraction. Biophys. J., 68, 19s-26s.
8. 4-. Biochemistry 34, 8960-8972.
9. Guilford, W.H., Dupuis, D.E., Warshaw, D.M., Waller, G.S., Trybus, K.M., and Lowey, S. (1998). Double-headed smooth and skeletal myosins generate displacements by cooperative action of the two heads. Biophys. J. 74, A225.
10. Gulick, A.M., and Rayment, I. (1997). Structural studies on myosin II: communication between distant protein domains. Bioessays 19, 561-569.
11. Gulick, A.M., Bauer, C.B., Thoden, J.B., and Rayment, I. (1997). X-ray structures of the MgADP, MgATPγS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain. Biochemistry 36, 11619-11628.
12. Hiratsuka, T. (1992). Spatial proximity of ATP-sensitive tryptophanyl residue(s) and Cys-697 in myosin ATPase. J. Biol. Chem. 267, 14949-14954.
13. Ho, G., and Chisholm, R.L. (1997). Substitution mutations in the myosin essential light chain lead to reduced actin-activated ATPase activity despite stoichiometric binding to the heavy chain. J. Biol. Chem. 272, 4522-4527.
14. Holmes, K.C. (1996). Muscle proteins - their actions and interactions. Curr. Opin. Struct. Biol. 6, 781-789.
15. Holmes, K.C. (1997). The swinging lever-arm hypothesis of muscle contraction. Curr. Biol. 7, R112-R118.
16. Holmes, K.C. (1998). Muscle contraction. In The Limits of Reductionism in Biology. Novartis Foundation Symposium 213 (Chichester: Wiley), pp. 76-92.
17. Houdusse, A., and Cohen, C. (1996). Structure of the regulatory domain of scallop myosin at 2Å resolution: implications for regulation. Structure 4, 21-32.
18. Huston, E.E., Grammer, J.C., and Yount, R.G. (1988). The flexibility of the myosin heavy chain: direct evidence that the region containing SH1 and SH2 can move 10Å under the influence of nucleotide binding. Biochemistry 27, 8945-8952.
19. Ishijima, A., Kojima, H., Funatsu, T., Tokunaga, M., Higuchi, H., Tanaka, H., and Yanagida, T. (1998). Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92, 161-171.
20. Johnson, K.A., and Taylor, E.W. (1978). Intermediate states of subfragment 1 and actosubfragment 1 ATPase: reevaluation of the mechanism. Biochemistry 17, 3432-3442.
21. Jones, T.A., Zou, J.-Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved experimental procedures for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
22. Jontes, J.D., and Milligan, R.A. (1997). Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis. J. Cell Biol. 139, 683-693.
23. Kleywegt, G.J., and Brünger, A.T. (1996). Checking your imagination: applications of the free R value. Structure 4, 897-904.
24. Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
25. Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163.
26. O'Reilly, D.R., Miller, L.K., and Luckow, V.A. (1992). Baculovirus Expression Vectors, A Laboratory Manual (New York: W. H. Freeman).
27. Otwinowski, Z., and Minor, W. (1993). Oscillation data reduction program. In Data Collection and Processing, L. Sawyer, N. Isaacs, and S. Bailey, eds. (Warrington, U.K.: CLRC Daresbury Laboratory), pp. 59-62.
28. Patterson, B., Ruppel, K.M., Wu, Y., and Spudich, J.A. (1997). Cold-sensitive mutants G680V and G691C of Dictyostelium myosin II confer dramatically different biochemical defects. J. Biol. Chem. 272, 27612-27617.
29. Perreault-Micale, C.L., Kalabokis, V.N., Nyitray, L., and Szent-Gyorgyi, A.G. (1996). Sequence variations in the surface loop near the nucleotide binding site modulate the ATP turnover rates of molluscan myosins. J. Muscle Res. Cell Motil. 17, 543-553.
30. Rayment, I. (1996). The structural basis of the myosin ATPase activity. J. Biol. Chem. 271, 15850-15853.
31. Rayment, I., Rypniewski, W.R., Schmidt-Base, K., Smith, R., Tomchick, D.R., Benning, M.M., Winkelmann, D.A., Wesenberg, G., and Holden, H.M. (1993a). Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261, 50-58.
32. Rayment, I., Holden, H.M., Whittaker, M., Yohn, C.B., Lorenz, M., Holmes, K.C., and Milligan, R.A. (1993b). Structure of the actin-myosin complex and its implications for muscle contraction. Science 261, 58-65.
33. Rayment, I., Holden, H.M., Sellers, J.R., Fananapazir, L., and Epstein, N.D. (1995). Structural interpretation of the mutations in the β-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy. Proc. Natl. Acad. Sci. USA 92, 3864-3868.
34. Rovner, A.S., Freyzon, Y., and Trybus, K.M. (1997). An insert in the motor domain determines the functional properties of expressed smooth muscle myosin isoforms. J. Muscle Res. Cell Motil. 18, 103-110.
35. Smith, C.A., and Rayment, I. (1996a). X-ray structure of the magnesium(II)·ADP·vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9Å resolution. Biochemistry 35, 5404-5417.
36. Smith, C.A., and Rayment, I. (1996b). Active site comparisons highlight structural similarities between myosin and other P-loop proteins. Biophys J. 70, 1590-1602.
37. Spudich, J.A. (1994). How molecular motors work. Nature 372, 515-518.
38. Sweeney, H.L., Rosenfeld, S.S., Brown, F., Faust, L., Smith, J., Xing, J., Stein, L.A., and Sellers, J.R. (1998). Kinetic tuning of myosin via a flexible loop adjacent to the nucleotide binding pocket. J. Biol. Chem. 273, 6262-6270.
39. Trybus, K.M. (1994). Regulation of express truncated smooth muscle myosins. Role of the essential light chain and tail length. J. Biol. Chem. 269, 20819-20822.
40. Vale, R.D. (1996). Switches, latches and amplifiers: common themes of G proteins and molecular motors. J. Cell Biol. 135, 291-302.
41. VanBuren, P., Waller, G.S., Harris, D.E., Trybus, K.M., Warshaw, D.M., and Lowey, S. (1994). The essential light chain is required for full force production by skeletal muscle myosin. Proc. Natl. Acad. Sci. USA 91, 12403-12407.
42. Whittaker, M., Wilson-Kubalek, E.M., Smith, J.E., Faust, L., Milligan, R.A., and Sweeney, H.L. (1995). A 35-Å movement of smooth muscle myosin on ADP release. Nature 378, 748-751.
43. Xie, X., Harrison, D.H., Schlichting, I., Sweet, R.M. Kalabokis, V.N., Szent-Gyorgyi, A.G., and Cohen, C. (1994). Structure of the regulatory domain of scallop myosin at 2.8Å resolution. Nature 368, 306-312.
44. Yount, R.G., Lawson, D., and Rayment, I. (1995). Is myosin a "back door" enzyme? Biophys. J. 68 (4 Suppl.), 44S-47S.