Structures of four Ca2+-bound troponin C at 2.0 Å resolution: Further insights into the Ca2+-switch int he calmodulin superfamily

Structure

Volumn 5, Issue 12, 1997, Pages 1695-1711

  Houdusse, Anne ^a   Love, Michael L ^a   Dominguez, Roberto ^a   Grabarek, Zenon ^b   Cohen, Carolyn ^a  

^a BRANDEIS UNIVERSITY   (United States)

^b BOSTON BIOMEDICAL RESEARCH INSTITUTE   (United States)

Author keywords

Ca2+ sensing proteins; Calmodulin; Muscle regulation; Troponin C

Indexed keywords

CALCIUM; CALMODULIN; TROPONIN C;

ANIMAL; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; CRYSTALLIZATION; METABOLISM; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; RABBIT; X RAY CRYSTALLOGRAPHY;

ANIMALS; BINDING SITES; CALCIUM; CALMODULIN; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RABBITS; TROPONIN C;

EID: 0031573485     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00315-8     Document Type: Article

References (54)

1. Sundaralingam, M., et al., & Wang, B.C. (1985). Molecular structure of troponin C from chicken skeletal muscle at 3.0 Å resolution. Science 227, 945-948.
2. 2+ state at 2.0 Å resolution. J. Biol. Chem. 263, 1628-1647.
3. Satyshur, K.A., Pyzalska, D., Greaser, M., Rao, S.T. & Sundaralingam, M. (1994). Structure of chicken skeletal muscle troponin C at 1.8 Å resolution. Acta Cryst. D 50, 40-49.
4. Herzberg, O. & James, M.N.G. (1988). Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 A resolution. J. Mol. Biol. 203, 761-779.
5. Babu, Y.S., et al., & Cook, W.J. (1985). Three-dimensional structure of calmodulin. Nature 315, 37-40.
6. Chattopadhyaya, R., Meador, W.E., Means, A.R. & Quiocho, F.A. (1992). Calmodulin structure refined at 1.7 Å. J. Mol. Biol. 228, 1177-1192.
7. Ban, C., Ramakrishnan, B., Ling, K.-Y., Kung, C. & Quiocho, F.A. (1994). Structure of the recombinant Paramecium tetraurelia calmodulin at 1.68 Å resolution. Acta Cryst. D 50, 50-63.
8. 2+-binding protein. II. Structure determination and general description. J. Biol. Chem. 248, 3313-3326.
9. 2+-induced conformational transition of troponin C. J. Biol. Chem. 261, 2638-2644.
10. Ikura, M., et al., & Bax, A. (1992). Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256, 632-638.
11. Meador, W.E., Means, A.R. & Quiocho, F.A. (1992). Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Science 257, 1251-1255.
12. Meador, W.E., Means, A.R. & Quiocho, F.A. (1993). Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science 262, 1718-1721.
13. Houdusse, A. & Cohen, C. (1995). Target sequence recognition by the calmodulin superfamily: implications from light chain binding to the regulatory domain of scallop myosin. Proc. Natl. Acad. Sci. USA 92, 10644-10647.
14. 2+-free calmodulin binding to unconventional myosins reveals how calmodulin acts as a regulatory switch. Structure 4, 1475-1490.
15. Cohen, C. (1975). The protein switch of muscle contraction. Sci. Am. 233, 36-45.
16. Leavis, P.C. & Gergely, J. (1984). Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction. CRC Crit. Rev. Biochem. 16, 235-305.
17. 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils. J. Biol. Chem. 257, 7678-7683.
18. Kuboniwa, H., et al., & Bax, A. (1995). Solution structure of calcium-free calmodulin. Nat. Struct. Biol. 2, 768-776.
19. 2+-induced conformational transition revealed by the solution structure of apo calmodulin. Nat. Struct. Biol. 2, 758-767.
20. 2+ saturated states. Nat. Struct. Biol. 2, 784-789.
21. 2+-saturated skeletal muscle troponin C. Biochem. 34, 1 5953-15964.
22. 2+-free forms of the N-terminal regulatory domain of troponin C. Biophys. J. Abst. 68, A359.
23. 2+. Identification of cleavage points. Biochim. Biophys. Acta. 671, 227-233.
24. 2+ binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem. 250, 4628-4633.
25. 2+ binding sites and interactions with troponin I and troponin T. J. Biol. Chem. 253, 5452-5459.
26. Swindells, M.B. & Ikura, M. (1996). Pre-formation of the semi-open conformation by the apo-calmodulin C-terminal domain and implications for binding IQ-motifs. Nat. Struct. Biol. 3, 501-504.
27. 2+ affinity. Eur. J. Biochem. 213, 599-604.
28. 2+-induced conformational transition of troponin C with site-directed mutants. Nature 345, 82-184.
29. Xie, X., et al., & Cohen, C. (1994). Structure of the regulatory domain of scallop myosin at 2.8 A resolution. Nature 368, (6469), 306-312.
30. Houdusse, A. & Cohen, C. (1996). Structure of the regulatory domain of scallop myosin at 2.0 Å resolution: implications for regulation. Structure 4, 21-32.
31. Gulati J., Babu, A., Su, H. & Zhang, Y.F. (1993). Identification of the regions conferring calmodulin-like properties to troponin C. J. Biol. Chem. 268, 11685-11690.
32. Grabarek, Z., Tao, T. & Gergely, J. (1992). Molecular mechanism of troponin-C function. J. Muscle Res. Cell Motil. 13, 383-393.
33. Farah, C.S. & Reinach, F.C. (1995). The troponin complex and regulation of muscle contraction. FASEB J. 9, 755-767.
34. Ingraham, R.H. & Swenson, C.A. (1984). Binary interactions of troponin subunits. J. Biol. Chem. 259, 9544-9548.
35. 2+ and troponin I to troponin C from rabbit skeletal muscle. Biophys. J. 48, 727-739.
36. Grabarek, Z., Drabikowski, W., Leavis, P.C., Rosenfeld, S.S. & Gergely, J. (1981). Proteolytic fragments of troponin C. Interactions with the other troponin subunits and biological activity. J. Biol. Chem. 256, 13121-13127.
37. Syska, H., Wilkinson, J.M., Grand, R.J. & Perry, S.V. (1976). The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit. Biochem. J. 153, 375-387.
38. Talbot, J.A. & Hodges, R.S. (1981). Synthetic studies on the inhibitory region of rabbit skeletal troponin I. Relationship of amino acid sequence to biological activity. J. Biol. Chem. 256, 2798-2802.
39. Farah, C.S., et al., & Reinach, F.C. (1994). Structural and regulatory functions of the NH2- and COOH-terminal regions of skeletal muscle troponin I. J. Biol. Chem. 269, 5230-5240.
40. Campbell, A.P. & Sykes, B.D. (1991). Interaction of troponin I and troponin C. Use of the two-dimensional nuclear magnetic resonance transferred nuclear Overhauser effect to determine the structure of the inhibitory troponin I peptide when bound to skeletal troponin C. J. Mol. Biol. 222, 405-421.
41. Kobayashi, T., Tao, T., Grabarek, Z., Gergely, J. & Collins, J.H. (1991). Cross-linking of residue 57 in the regulatory domain of a mutant rabbit skeletal muscle troponin C to the inhibitory region of troponin I. J. Biol. Chem. 266, 13746-13751.
42. Matthews, B.W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
43. Otwinowski, Z. (1993). DENZO: an oscillation data processing program for macromolecular crystallography. Yale University, New Haven, CT.
44. Otwinowski, Z. (1993). SCALEPACK: Software for the scaling together of integrated intensities measured on a number of separate diffraction images. Yale University, New Haven, CT.
45. 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.
46. Otwinowsky, Z. (1991). Proceedings of the CCP4 Study Weekend. (Wolf, W., Evans, P.R. & Leslie, A.G.W., eds), Daresbury Laboratory, Warrington, UK.
47. Brünger, AT., Kuriyan, J. & Karplus, M. (1987). Crystallographic R-factor refinement by molecular dynamics. Science 235, 458-460.
48. Lamzin, V.S. & Wilson, K.S. (1993). Automated refinement of protein models. Acta Cryst. D49, 129-147.
49. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
50. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
51. Navaza, J. (1994). AMoRe: an Automated Package for Molecular Replacement. Acta Cryst. A 50, 157-163.
52. Bernstein, F.C., et al., & Tasumi, M. (1977). The protein databank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
53. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
54. Brünger, A.T. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 335, 472-474.