Calcium binding to the regulatory domain of skeletal muscle troponin C induces a highly constrained open conformation

Journal of Molecular Biology

Volumn 281, Issue 3, 1998, Pages 445-452

  She, Mingda ^a   Xing, Jun ^b   Dong, Wen Ji ^b   Umeda, Patrick K ^c   Cheung, Herbert C ^a,b  

^a Department of Physics 35294 ^*  (United States)

^b UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^c UNIVERSITY OF ALABAMA SCHOOL OF MEDICINE   (United States)

Author keywords

Activation; Calcium; Conformation; Distance; Troponin C

Indexed keywords

CALCIUM; CALCIUM BINDING PROTEIN; CYSTEINE; MUSCLE PROTEIN; MUTANT PROTEIN; SULFONIC ACID DERIVATIVE; TROPONIN C; TRYPTOPHAN;

AMINO TERMINAL SEQUENCE; ARTICLE; CALCIUM BINDING; ENERGY TRANSFER; FLUORESCENCE ANALYSIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; SKELETAL MUSCLE;

EID: 0032555762     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1933     Document Type: Article

References (26)

1. Aguirre R., Lin S.-H., Gonsoulin F., Wang C.-K., Cheung H.C. Characterization of the ethenoadenosine diphosphate binding site of myosin subfragment 1. Biochemistry. 28:1989;799-807
2. Cheung H.C., Wang C.-K., Malik N.A. Interaction of troponin subunits free energy of binary and tertiary complexes. Biochemistry. 26:1987;5904-5907
3. Dale R.E., Eisinger J., Blumberg W.E. The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer. Biophys. J. 26:1979;161-193
4. Dong W.-J., Chandra M., Xing J., She M., Solaro R.J., Cheung H.C. Phosphorylation-induced distance change in a cardiac muscle troponin I mutant. Biochemistry. 36:1997;6754-6761
5. Gagné S.M., Tsuda S., Li M.X., Chandra M., Smillie L.B., Sykes B.D. Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C. Protein Sci. 3:1994;1961-1974
6. Gagné S.M., Tsuda S., Li M.X., Smillie L.B., Sykes B.D. Structures of the troponin C regulatory domains in the apo and calcium-saturated states. Nature Struct. Biol. 2:1995;784-788
7. Gagné S.M., Li M.X., Sykes B.D. Mechanism of direct coupling between binding and induced structural change in regulatory calcium binding proteins. Biochemistry. 36:1997;4386-4392
8. Grabarek Z., Tan R.-Y., Wang J., Tao T., Gergely J. Inhibition of mutant TnC activity by an intra-domain disulphide bind. Nature. 345:1990;132-135
9. Herzberg O., James M.N.G. Structure of the calcium regulatory protein troponin-C at 2.8 Å resolution. Nature. 313:1985;653-659
10. 2+-induced conformational transition of troponin C. J. Mol. Biol. 261:1986;653-659
11. Lakowicz J.R., Gryczynski I., Cheung H.C., Wang C.-K., Johnson M.L., Joshi N. Distance distribution in proteins recovered by using frequency-domain fluorometry. Application to troponin I and its complex with troponin C. Biochemistry. 27:1988;9149-9160
12. Lakowicz J.R., Gryczynski I., Wiczk W., Laczko G., Prendergast F.G., Johnson M.L. Conformational distributions of mellitin in water/methanol mixtures from frequency-domain measurements of nonradiative energy transfer. Biophys. Chem. 36:1990;99-115
13. Potter J.D., Gergely J. The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar ATPase. J. Biol. Chem. 250:1975;4628-4633
14. 2+affinity. Biochemistry. 31:1992;6545-6553
15. 2-adrenergic receptor. Extending the ternary complex model. J. Biol. Chem. 268:1993;4625-4636
16. She M., Dong W.-J., Umeda P.K., Cheung H.C. Time-resolved fluorescence study of the single tryptophans of engineered skeletal muscle troponin C. Biophys. J. 73:1997;1042-1055
17. She M., Dong W.-J., Umeda P.K., Cheung H.C. Tryptophan mutants of troponin C from skeletal muscle. An optical probe of the regulatory domain. Eur. J. Biochem. 252:1998;600-607
18. Slupsky C.M., Sykes B.D. NMR solution studies of calcium-saturated skeletal muscle troponin C. Biochemistry. 34:1995;15953-15964
19. Sundaralingam M., Berstrom R., Strasburg G., Rao R.T., Roychowdbury R., Greaser M., Wang B.-C. Molecular structure of troponin C from chicken skeletal muscle at 3-Ångstrom resolution. Science. 227:1985;945-948
20. Tao T., Gong B.-J., Leavis P.C. Calcium-induced movement of troponin-I relative to actin in skeletal muscle thin filaments. Science. 247:1990;1339-1341
21. bexcitation bands. Photochem. Photobiol. 25:1977;441-444
22. Wang C.-K., Cheung H.C. Energetics of the binding of calcium and troponin I to troponin C from rabbit skeletal muscle. Biophys. J. 48:1985;727-739
23. Wang C.-K., Cheung H.C. Proximity relationship in the binary complex formed between troponin I and troponin C. J. Mol. Biol. 191:1986;509-521
24. 2+-triggered conformational transition in troponin C. Proc. Natl Acad. Sci. USA. 89:1992;11814-11817
25. Wu P., Brand L. Orientation factor in steady state and time-resolved resonance energy transfer measurements. Biochemistry. 31:1992;7939-7947
26. 2+sites on troponin C in the regulation of muscle contraction preparation and properties of troponin C depleted myofibrils. J. Biol. Chem. 257:1982;7678-7683