메뉴 건너뛰기




Volumn 43, Issue 40, 2004, Pages 12846-12854

SERCA structural dynamics induced by ATP and calcium

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; CALCIUM; ENZYME INHIBITION; ENZYMES; MOLECULAR ORIENTATION; MONOMERS; OLIGOMERS; PHOSPHORESCENCE; PROTEINS; X RAY CRYSTALLOGRAPHY;

EID: 4944247857     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0489457     Document Type: Article
Times cited : (23)

References (41)
  • 1
    • 0021894467 scopus 로고
    • Mechanism of calcium transport
    • Inesi, G. (1985) Mechanism of calcium transport, Annu. Rev. Physiol. 47, 573-601.
    • (1985) Annu. Rev. Physiol. , vol.47 , pp. 573-601
    • Inesi, G.1
  • 2
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution, Nature 405, 647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 3
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima, C., and Nomura, H. (2002) Structural changes in the calcium pump accompanying the dissociation of calcium, Nature 418, 605-611.
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 4
    • 0033166241 scopus 로고    scopus 로고
    • Comparison of H+-ATPase and Ca2+-ATPase suggests that a large conformational change initiates P-type ion pump reaction cycles
    • Stokes, D. L., Auer, M., Zhang, P., and Kuhlbrandt, W. (1999) Comparison of H+-ATPase and Ca2+-ATPase suggests that a large conformational change initiates P-type ion pump reaction cycles, Curr. Biol. 9, 672-679.
    • (1999) Curr. Biol. , vol.9 , pp. 672-679
    • Stokes, D.L.1    Auer, M.2    Zhang, P.3    Kuhlbrandt, W.4
  • 5
    • 0037063730 scopus 로고    scopus 로고
    • Ca(2+)-ATPase structure in the E1 and E2 conformations: Mechanism, helix-helix and helix-lipid interactions
    • Lee, A. G. (2002) Ca(2+)-ATPase structure in the E1 and E2 conformations: Mechanism, helix-helix and helix-lipid interactions, Biochim. Biophys. Acta 1565, 246-266.
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 246-266
    • Lee, A.G.1
  • 6
    • 0036300446 scopus 로고    scopus 로고
    • A structural model for the catalytic cycle of Ca(2+)-ATPase
    • Xu, C., Rice, W. J., He, W., and Stokes, D. L. (2002) A structural model for the catalytic cycle of Ca(2+)-ATPase, J. Mol. Biol. 316, 201-211.
    • (2002) J. Mol. Biol. , vol.316 , pp. 201-211
    • Xu, C.1    Rice, W.J.2    He, W.3    Stokes, D.L.4
  • 7
    • 0025932305 scopus 로고
    • The effect of high pressure on the conformation, interactions and activity of the Ca(2+)-ATPase of sarcoplasmic reticulum
    • Jona, I., and Martonosi, A. (1991) The effect of high pressure on the conformation, interactions and activity of the Ca(2+)-ATPase of sarcoplasmic reticulum, Biochim. Biophys. Acta 1070, 355-373.
    • (1991) Biochim. Biophys. Acta , vol.1070 , pp. 355-373
    • Jona, I.1    Martonosi, A.2
  • 8
    • 0028179410 scopus 로고
    • Conformation of Ca(2+)-ATPase in two crystal forms. Effects of Ca2+, thapsigargin, adenosine 5′-(β,γ-methylene)triphosphate), and chromium(III)-ATP on crystallization
    • Stokes, D. L., and Lacapere, J. J. (1994) Conformation of Ca(2+)-ATPase in two crystal forms. Effects of Ca2+, thapsigargin, adenosine 5′-(β,γ-methylene)triphosphate), and chromium(III)-ATP on crystallization, J. Biol. Chem. 269, 11606-11613.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11606-11613
    • Stokes, D.L.1    Lacapere, J.J.2
  • 9
    • 0032562141 scopus 로고    scopus 로고
    • Differential effects of general anesthetics on the quaternary structure of the Ca-ATPases of cardiac and skeletal sarcoplasmic reticulum
    • Kutchai, H., Geddis, L. M., Jones, L. R., and Thomas, D. D. (1998) Differential effects of general anesthetics on the quaternary structure of the Ca-ATPases of cardiac and skeletal sarcoplasmic reticulum, Biochemistry 37, 2410-2421.
    • (1998) Biochemistry , vol.37 , pp. 2410-2421
    • Kutchai, H.1    Geddis, L.M.2    Jones, L.R.3    Thomas, D.D.4
  • 10
    • 0025319233 scopus 로고
    • Rotational dynamics of the Ca-ATPase in sarcoplasmic reticulum studied by time-resolved phosphorescence anisotropy
    • Birmachu, W., and Thomas, D. D. (1990) Rotational dynamics of the Ca-ATPase in sarcoplasmic reticulum studied by time-resolved phosphorescence anisotropy, Biochemistry 29, 3904-3914.
    • (1990) Biochemistry , vol.29 , pp. 3904-3914
    • Birmachu, W.1    Thomas, D.D.2
  • 11
    • 0028114256 scopus 로고
    • Halothane and cyclopiazonic acid modulate Ca-ATPase oligomeric state and function in sarcoplasmic reticulum
    • Karon, B. S., Mahaney, J. E., and Thomas, D. D. (1994) Halothane and cyclopiazonic acid modulate Ca-ATPase oligomeric state and function in sarcoplasmic reticulum, Biochemistry 33, 13928-13937.
    • (1994) Biochemistry , vol.33 , pp. 13928-13937
    • Karon, B.S.1    Mahaney, J.E.2    Thomas, D.D.3
  • 12
    • 0028096951 scopus 로고
    • Hexanol and lidocaine affect the oligomeric state of the Ca-ATPase of sarcoplasmic reticulum
    • Kutchai, H., Mahaney, J. E., Geddis, L. M., and Thomas, D. D. (1994) Hexanol and lidocaine affect the oligomeric state of the Ca-ATPase of sarcoplasmic reticulum, Biochemistry 33, 13208-13222.
    • (1994) Biochemistry , vol.33 , pp. 13208-13222
    • Kutchai, H.1    Mahaney, J.E.2    Geddis, L.M.3    Thomas, D.D.4
  • 13
    • 0027501738 scopus 로고
    • Protein and lipid rotational dynamics in cardiac and skeletal sarcoplasmic reticulum detected by EPR and phosphorescence anisotropy
    • Birmachu, W., Voss, J. C., Louis, C. F., and Thomas, D. D. (1993) Protein and lipid rotational dynamics in cardiac and skeletal sarcoplasmic reticulum detected by EPR and phosphorescence anisotropy, Biochemistry 32, 9445-9453.
    • (1993) Biochemistry , vol.32 , pp. 9445-9453
    • Birmachu, W.1    Voss, J.C.2    Louis, C.F.3    Thomas, D.D.4
  • 14
    • 0027327973 scopus 로고
    • Molecular mechanism of Ca-ATPase activation by halothane in sarcoplasmic reticulum
    • Karon, B. S., and Thomas, D. D. (1993) Molecular mechanism of Ca-ATPase activation by halothane in sarcoplasmic reticulum, Biochemistry 32, 7503-7511.
    • (1993) Biochemistry , vol.32 , pp. 7503-7511
    • Karon, B.S.1    Thomas, D.D.2
  • 15
    • 0025720013 scopus 로고
    • Effects of melittin on molecular dynamics and Ca-ATPase activity in sarcoplasmic reticulum membranes: Time-resolved optical anisotropy
    • Voss, J., Birmachu, W., Hussey, D. M., and Thomas, D. D. (1991) Effects of melittin on molecular dynamics and Ca-ATPase activity in sarcoplasmic reticulum membranes: Time-resolved optical anisotropy, Biochemistry 30, 7498-7506.
    • (1991) Biochemistry , vol.30 , pp. 7498-7506
    • Voss, J.1    Birmachu, W.2    Hussey, D.M.3    Thomas, D.D.4
  • 16
    • 0014483568 scopus 로고
    • ATP dependent conformational change in "spin labelled" sarcoplasmic reticulum
    • Landgraf, W. C., and Inesi, G. (1969) ATP dependent conformational change in "spin labelled" sarcoplasmic reticulum, Arch. Biochem. Biophys. 130, 111-118.
    • (1969) Arch. Biochem. Biophys. , vol.130 , pp. 111-118
    • Landgraf, W.C.1    Inesi, G.2
  • 17
    • 0026670180 scopus 로고
    • Resolved conformational states of spin-labeled Ca-ATPase during the enzymatic cycle
    • Lewis, S. M., and Thomas, D. D. (1992) Resolved conformational states of spin-labeled Ca-ATPase during the enzymatic cycle, Biochemistry 31, 7381-7389.
    • (1992) Biochemistry , vol.31 , pp. 7381-7389
    • Lewis, S.M.1    Thomas, D.D.2
  • 18
    • 0020787375 scopus 로고
    • Segmental motion and rotational diffusion of the Ca2+-translocating adenosine triphosphatase of sarcoplasmic reticulum, measured by time-resolved phosphorescence depolarization
    • Speirs, A., Moore, C. H., Boxer, D. H., and Garland, P. B. (1983) Segmental motion and rotational diffusion of the Ca2+-translocating adenosine triphosphatase of sarcoplasmic reticulum, measured by time-resolved phosphorescence depolarization, Biochem. J. 213, 67-74.
    • (1983) Biochem. J. , vol.213 , pp. 67-74
    • Speirs, A.1    Moore, C.H.2    Boxer, D.H.3    Garland, P.B.4
  • 19
    • 0019034484 scopus 로고
    • Highly purified sarcoplasmic reticulum vesicles are devoid of Ca2+-independent ('basal') ATPase activity
    • Fernandez, J. L., Rosemblatt, M., and Hidalgo, C. (1980) Highly purified sarcoplasmic reticulum vesicles are devoid of Ca2+-independent ('basal') ATPase activity, Biochim. Biophys. Acta 599, 552-568.
    • (1980) Biochim. Biophys. Acta , vol.599 , pp. 552-568
    • Fernandez, J.L.1    Rosemblatt, M.2    Hidalgo, C.3
  • 20
    • 0024573346 scopus 로고
    • Conformational transitions in the calcium adenosinetriphosphatase studied by time-resolved fluorescence resonance energy transfer
    • Birmachu, W., Nisswandt, F. L., and Thomas, D. D. (1989) Conformational transitions in the calcium adenosinetriphosphatase studied by time-resolved fluorescence resonance energy transfer, Biochemistry 28, 3940-3947.
    • (1989) Biochemistry , vol.28 , pp. 3940-3947
    • Birmachu, W.1    Nisswandt, F.L.2    Thomas, D.D.3
  • 21
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall, A. G., Bardawill, C. J., and David, M. M. (1948) Determination of serum proteins by means of the biuret reaction, J. Biol. Chem. 177, 751-766.
    • (1948) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 22
    • 0037461273 scopus 로고    scopus 로고
    • Defining the molecular components of calcium transport regulation in a reconstituted membrane system
    • Reddy, L. G., Cornea, R. L., Winters, D. L., McKenna, E., and Thomas, D. D. (2003) Defining the molecular components of calcium transport regulation in a reconstituted membrane system, Biochemistry 42, 4585-4592.
    • (2003) Biochemistry , vol.42 , pp. 4585-4592
    • Reddy, L.G.1    Cornea, R.L.2    Winters, D.L.3    McKenna, E.4    Thomas, D.D.5
  • 23
    • 0024276822 scopus 로고
    • Microsecond rotational dynamics of phosphorescent-labeled muscle cross-bridges
    • Ludescher, R. D., and Thomas, D. D. (1988) Microsecond rotational dynamics of phosphorescent-labeled muscle cross-bridges, Biochemistry 27, 3343-3351.
    • (1988) Biochemistry , vol.27 , pp. 3343-3351
    • Ludescher, R.D.1    Thomas, D.D.2
  • 24
    • 0024201809 scopus 로고
    • Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands
    • Fabiato, A. (1988) Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands, Methods Enzymol 157, 378-417.
    • (1988) Methods Enzymol. , vol.157 , pp. 378-417
    • Fabiato, A.1
  • 25
    • 0028861593 scopus 로고
    • Self-association accompanies inhibition of Ca-ATPase by thapsigargin
    • Mersol, J. V., Kutchai, H., Mahaney, J. E., and Thomas, D. D. (1995) Self-association accompanies inhibition of Ca-ATPase by thapsigargin, Biophys. J. 68, 208-215.
    • (1995) Biophys. J. , vol.68 , pp. 208-215
    • Mersol, J.V.1    Kutchai, H.2    Mahaney, J.E.3    Thomas, D.D.4
  • 26
    • 0029966678 scopus 로고    scopus 로고
    • Microsecond rotational dynamics of actin: Spectroscopic detection and theoretical simulation
    • Prochniewicz, E., Zhang, Q., Howard, E. C., and Thomas, D. D. (1996) Microsecond rotational dynamics of actin: Spectroscopic detection and theoretical simulation, J. Mol. Biol. 255, 446-457.
    • (1996) J. Mol. Biol. , vol.255 , pp. 446-457
    • Prochniewicz, E.1    Zhang, Q.2    Howard, E.C.3    Thomas, D.D.4
  • 27
    • 0001545374 scopus 로고
    • Theory of fluorescence depolarization in macromolecules and membranes
    • Szabo, A. (1984) Theory of fluorescence depolarization in macromolecules and membranes, J. Chem. Phys. 81, 150-167.
    • (1984) J. Chem. Phys. , vol.81 , pp. 150-167
    • Szabo, A.1
  • 28
    • 0024570142 scopus 로고
    • Changes in the steady-state fluorescence anisotropy of N-iodo-acetyl-N′-(5-sulfo-1-naphthyl)ethylenediamine attached to the specific thiol of sarcoplasmic reticulum Ca2+-ATPase throughout the catalytic cycle
    • Suzuki, H., Obara, M., Kubo, K., and Kanazawa, T. (1989) Changes in the steady-state fluorescence anisotropy of N-iodo-acetyl-N′-(5-sulfo-1- naphthyl)ethylenediamine attached to the specific thiol of sarcoplasmic reticulum Ca2+-ATPase throughout the catalytic cycle, J. Biol. Chem. 264, 920-927.
    • (1989) J. Biol. Chem. , vol.264 , pp. 920-927
    • Suzuki, H.1    Obara, M.2    Kubo, K.3    Kanazawa, T.4
  • 29
    • 3042730955 scopus 로고    scopus 로고
    • Direct detection of phospholamban and SERCA interaction in membranes using fluroescence resonance energy transfer
    • Mueller, B., Karim, C. B., Negrashov, I. V., Kutchai, H., and Thomas, D. D. (2004) Direct detection of phospholamban and SERCA interaction in membranes using fluroescence resonance energy transfer. Biochemistry 43, 8754-8765.
    • (2004) Biochemistry , vol.43 , pp. 8754-8765
    • Mueller, B.1    Karim, C.B.2    Negrashov, I.V.3    Kutchai, H.4    Thomas, D.D.5
  • 30
    • 0025950765 scopus 로고
    • Microsecond rotational dynamics of spin-labeled Ca-ATPase during enzymatic cycling initiated by photolysis of caged ATP
    • Lewis, S. M., and Thomas, D. D. (1991) Microsecond rotational dynamics of spin-labeled Ca-ATPase during enzymatic cycling initiated by photolysis of caged ATP, Biochemistry 30, 8331-8339.
    • (1991) Biochemistry , vol.30 , pp. 8331-8339
    • Lewis, S.M.1    Thomas, D.D.2
  • 31
    • 0027058497 scopus 로고
    • Effects of melittin on lipid-protein interactions in sarcoplasmic reticulum membranes
    • Mahaney, J. E., Kleinschmidt, J., Marsh, D., and Thomas, D. D. (1992) Effects of melittin on lipid-protein interactions in sarcoplasmic reticulum membranes, Biophys. J. 63, 1513-1522.
    • (1992) Biophys. J. , vol.63 , pp. 1513-1522
    • Mahaney, J.E.1    Kleinschmidt, J.2    Marsh, D.3    Thomas, D.D.4
  • 32
    • 0028899386 scopus 로고
    • Mechanism of Ca-ATPase inhibition by melittin in skeletal sarcoplasmic reticulum
    • Voss, J. C., Mahaney, J. E., and Thomas, D. D. (1995) Mechanism of Ca-ATPase inhibition by melittin in skeletal sarcoplasmic reticulum, Biochemistry 34, 930-939.
    • (1995) Biochemistry , vol.34 , pp. 930-939
    • Voss, J.C.1    Mahaney, J.E.2    Thomas, D.D.3
  • 33
    • 0033143058 scopus 로고    scopus 로고
    • Characteristics of the interaction of melittin with sarcoplasmic reticulum membranes
    • Shorina, E. A., Mast, N. V., Storey, K. B., Lopina, O. D., and Rubtsov, A. M. (1999) Characteristics of the interaction of melittin with sarcoplasmic reticulum membranes, Biochemistry (Moscow) 64, 705-713.
    • (1999) Biochemistry (Moscow) , vol.64 , pp. 705-713
    • Shorina, E.A.1    Mast, N.V.2    Storey, K.B.3    Lopina, O.D.4    Rubtsov, A.M.5
  • 34
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • Sorensen, T. L., Moller, J. V., and Nissen, P. (2004) Phosphoryl transfer and calcium ion occlusion in the calcium pump, Science 304, 1672-165.
    • (2004) Science , vol.304 , pp. 1672-1165
    • Sorensen, T.L.1    Moller, J.V.2    Nissen, P.3
  • 36
    • 0028922449 scopus 로고
    • Conformational transitions of the sarcoplasmic reticulum Ca-ATPase studied by time-resolved EPR and quenched-flow kinetics
    • Mahaney, J. E., Froechlich, J. P., and Thomas, D. D. (1995) Conformational transitions of the sarcoplasmic reticulum Ca-ATPase studied by time-resolved EPR and quenched-flow kinetics, Biochemistry 34, 4864-7489.
    • (1995) Biochemistry , vol.34 , pp. 4864-7489
    • Mahaney, J.E.1    Froechlich, J.P.2    Thomas, D.D.3
  • 37
    • 0024457094 scopus 로고
    • Independent flexible motion of submolecular domains of the Ca2+, Mg2+- ATPase of sarco-plasmic reticulum measured by time-resolved fluorescence depo-larization of site-specifically attached probes
    • Suzuki, S., Kawato, S., Kouyama, T., Kinosita, K., Jr., Ikegami, A., and Kawakita, M. (1989) Independent flexible motion of submolecular domains of the Ca2+, Mg2+- ATPase of sarco-plasmic reticulum measured by time-resolved fluorescence depo-larization of site-specifically attached probes, Biochemistry 28, 7734-7740.
    • (1989) Biochemistry , vol.28 , pp. 7734-7740
    • Suzuki, S.1    Kawato, S.2    Kouyama, T.3    Kinosita Jr., K.4    Ikegami, A.5    Kawakita, M.6
  • 38
    • 0022433581 scopus 로고
    • Conformational changes in the (Ca2+ + Mg2+)-ATPase of sarcoplasmic reticulum detected using phosphorescence polarization
    • Restall, C. J., Coke, M., Murray, E. K., and Chapman, D. (1985) Conformational changes in the (Ca2+ + Mg2+)-ATPase of sarcoplasmic reticulum detected using phosphorescence polarization, Biochim. Biophys. Acta 813, 96-102.
    • (1985) Biochim. Biophys. Acta , vol.813 , pp. 96-102
    • Restall, C.J.1    Coke, M.2    Murray, E.K.3    Chapman, D.4
  • 39
    • 0028321788 scopus 로고
    • The physical mechanism of calcium pump regulation in the heart
    • Voss, J., Jones, L. R., and Thomas, D. D. (1994) The physical mechanism of calcium pump regulation in the heart, Biophys. J. 67, 190-196.
    • (1994) Biophys. J. , vol.67 , pp. 190-196
    • Voss, J.1    Jones, L.R.2    Thomas, D.D.3
  • 40
    • 0032558973 scopus 로고    scopus 로고
    • Enhanced rotational dynamics of the phosphorylation domain of the Ca-ATPase upon calcium activation
    • Huang, S., and Squier, T. C. (1998) Enhanced rotational dynamics of the phosphorylation domain of the Ca-ATPase upon calcium activation, Biochemistry 37, 18064-18073.
    • (1998) Biochemistry , vol.37 , pp. 18064-18073
    • Huang, S.1    Squier, T.C.2
  • 41
    • 0031736237 scopus 로고    scopus 로고
    • Direct spectroscopic detection of molecular dynamics and interactions of the calcium pump and phospholamban
    • Thomas, D. D., Reddy, L. G., Karim, C. B., Li, M., Cornea, R., Autry, J. M., Jones, L. R., and Stamm, J. (1998) Direct spectroscopic detection of molecular dynamics and interactions of the calcium pump and phospholamban, Ann. N. Y. Acad. Sci. 853, 186-194.
    • (1998) Ann. N. Y. Acad. Sci. , vol.853 , pp. 186-194
    • Thomas, D.D.1    Reddy, L.G.2    Karim, C.B.3    Li, M.4    Cornea, R.5    Autry, J.M.6    Jones, L.R.7    Stamm, J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.