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Volumn 47, Issue 15, 2008, Pages 4369-4376

Structural characterization of Ca2+-ATPase-bound phospholamban in lipid bilayers by solid-state nuclear magnetic resonance (NMR) spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CHARACTERIZATION; COMPUTER SIMULATION; CONFORMATIONS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLID STATE REACTIONS;

EID: 42049119152     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7024194     Document Type: Article
Times cited : (50)

References (60)
  • 1
    • 0031722958 scopus 로고    scopus 로고
    • Phospholamban: Protein structure, mechanism of action, and role in cardiac function
    • Simmerman, H. K. B., and Jones, L. R. (1998) Phospholamban: Protein structure, mechanism of action, and role in cardiac function. Physiol. Rev. 78, 921-947.
    • (1998) Physiol. Rev , vol.78 , pp. 921-947
    • Simmerman, H.K.B.1    Jones, L.R.2
  • 2
    • 0016689752 scopus 로고
    • Phosphorylation of a 22,000-dalton component of cardiac sarcoplasmic reticulum by adenosine 3′-5′-monophosphate-dependent protein kinase
    • Tada, M., Kirchberger, M. A., and Katz, A. M. (1975) Phosphorylation of a 22,000-dalton component of cardiac sarcoplasmic reticulum by adenosine 3′-5′-monophosphate-dependent protein kinase. J. Biol. Chem. 250, 2640-2647.
    • (1975) J. Biol. Chem , vol.250 , pp. 2640-2647
    • Tada, M.1    Kirchberger, M.A.2    Katz, A.M.3
  • 3
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: A crucial regulator of cardiac contractility
    • MacLennan, D. H., and Kranias, E. G. (2003) Phospholamban: A crucial regulator of cardiac contractility. Nat. Rev. Mol. Cell Biol. 4, 566-577.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 4
    • 34047219171 scopus 로고    scopus 로고
    • SERCA pump isoforms: Their role in calcium transport and disease
    • Periasamy, M., and Kalyanasundaram, A. (2007) SERCA pump isoforms: Their role in calcium transport and disease. Muscle Nerve 35, 430-442.
    • (2007) Muscle Nerve , vol.35 , pp. 430-442
    • Periasamy, M.1    Kalyanasundaram, A.2
  • 5
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405, 647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 6
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl Transfer and Calcium Ion Occlusion in the Calcium Pump
    • Sorensen, T. L.-M., Moller, J. V., and Nissen, P. (2004) Phosphoryl Transfer and Calcium Ion Occlusion in the Calcium Pump. Science 304, 1672-1675.
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sorensen, T.L.-M.1    Moller, J.V.2    Nissen, P.3
  • 7
    • 11144330054 scopus 로고    scopus 로고
    • Dephosphorylation of the calcium pump coupled to counterion occlusion
    • Olesen, C., Sorensen, T. L. M., Nielsen, R. C., Moller, J. V., and Nissen, P. (2004) Dephosphorylation of the calcium pump coupled to counterion occlusion. Science 306, 2251-2255.
    • (2004) Science , vol.306 , pp. 2251-2255
    • Olesen, C.1    Sorensen, T.L.M.2    Nielsen, R.C.3    Moller, J.V.4    Nissen, P.5
  • 8
    • 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
  • 9
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • Toyoshima, C., and Mizutani, T. (2004) Crystal structure of the calcium pump with a bound ATP analogue. Nature 430, 529-535.
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 11
    • 25144453329 scopus 로고    scopus 로고
    • Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy
    • Andronesi, O. C., Becker, S., Seidel, K., Heise, H., Young, H. S., and Baldus, M. (2005) Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy. J. Am. Chem. Soc. 127, 12965-12974.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 12965-12974
    • Andronesi, O.C.1    Becker, S.2    Seidel, K.3    Heise, H.4    Young, H.S.5    Baldus, M.6
  • 13
    • 33748479782 scopus 로고    scopus 로고
    • Structural dynamics and topology of phospholamban in oriented lipid bilayers using multidimensional solid-state NMR
    • Traaseth, N. J., Buffy, J. J., Zamoon, J., and Veglia, G. (2006) Structural dynamics and topology of phospholamban in oriented lipid bilayers using multidimensional solid-state NMR. Biochemistry 45, 13827-13834.
    • (2006) Biochemistry , vol.45 , pp. 13827-13834
    • Traaseth, N.J.1    Buffy, J.J.2    Zamoon, J.3    Veglia, G.4
  • 14
    • 0141530952 scopus 로고    scopus 로고
    • NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles
    • Zamoon, J., Mascioni, A., Thomas, D. D., and Veglia, G. (2003) NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles. Biophys. J. 85, 2589-2598.
    • (2003) Biophys. J , vol.85 , pp. 2589-2598
    • Zamoon, J.1    Mascioni, A.2    Thomas, D.D.3    Veglia, G.4
  • 15
    • 0035834520 scopus 로고    scopus 로고
    • Helical structure of phospholamban in membrane bilayers
    • Smith, S. O., Kawakami, T., Liu, W., Ziliox, M., and Aimoto, S. (2001) Helical structure of phospholamban in membrane bilayers. J. Mol. Biol. 313, 1139-1148.
    • (2001) J. Mol. Biol , vol.313 , pp. 1139-1148
    • Smith, S.O.1    Kawakami, T.2    Liu, W.3    Ziliox, M.4    Aimoto, S.5
  • 16
    • 23344441824 scopus 로고    scopus 로고
    • The structure of phospholamban pentamer reveals a channel-like architecture in membranes
    • Oxenoid, K., and Chou, J. J. (2005) The structure of phospholamban pentamer reveals a channel-like architecture in membranes. Proc. Natl. Acad. Sci. U.S.A. 102, 10870-10875.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 10870-10875
    • Oxenoid, K.1    Chou, J.J.2
  • 18
    • 0030989981 scopus 로고    scopus 로고
    • Phospholamban inhibitory function is activated by depolymerization
    • Kimura, Y., Kurzydlowski, K., Tada, M., and MacLennan, D. H. (1997) Phospholamban inhibitory function is activated by depolymerization. J. Biol. Chem. 272, 15061-15064.
    • (1997) J. Biol. Chem , vol.272 , pp. 15061-15064
    • Kimura, Y.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 21
    • 0032755399 scopus 로고    scopus 로고
    • 2+-ATPase forms a functional interaction site with phospholamban - Evidence for physical, interactions at other sites
    • 2+-ATPase forms a functional interaction site with phospholamban - Evidence for physical, interactions at other sites. J. Biol. Chem. 274, 32855-32862.
    • (1999) J. Biol. Chem , vol.274 , pp. 32855-32862
    • Asahi, M.1    Kimura, Y.2    Kurzydlowski, R.3    Tada, M.4    MacLennan, D.H.5
  • 22
    • 0028168416 scopus 로고
    • 2+-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban
    • 2+-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban. J. Biol. Chem. 269, 22929-22932.
    • (1994) J. Biol. Chem , vol.269 , pp. 22929-22932
    • Toyofuku, T.1    Kurzydlowski, K.2    Tada, M.3    Maclennan, D.H.4
  • 24
    • 0037008735 scopus 로고    scopus 로고
    • 2+ pump revealed by intermolecular thiol cross-linking
    • 2+ pump revealed by intermolecular thiol cross-linking. J. Biol. Chem. 277, 28319-28329.
    • (2002) J. Biol. Chem , vol.277 , pp. 28319-28329
    • Jones, L.R.1    Cornea, R.L.2    Chen, Z.H.3
  • 28
    • 33744921916 scopus 로고    scopus 로고
    • 2+ pump of cardiac sarcoplasmic reticulum to probe spatial and functional interactions within the transmembrane domain
    • 2+ pump of cardiac sarcoplasmic reticulum to probe spatial and functional interactions within the transmembrane domain. J. Biol. Chem. 281, 14163-14172.
    • (2006) J. Biol. Chem , vol.281 , pp. 14163-14172
    • Chen, Z.H.1    Akin, B.L.2    Stokes, D.L.3    Jones, L.R.4
  • 30
    • 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, T. L., Karim, C. B., and Thomas, D. D. (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
  • 31
    • 3042730955 scopus 로고    scopus 로고
    • Direct detection of phospholamban and sarcoplasmic reticulum Ca-ATPase interaction in membranes using fluorescence resonance energy transfers
    • Mueller, B., Karim, C. B., Negrashov, I. V., Kutchai, H., and Thomas, D. D. (2004) Direct detection of phospholamban and sarcoplasmic reticulum Ca-ATPase interaction in membranes using fluorescence resonance energy transfers. 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
  • 32
    • 12244255136 scopus 로고    scopus 로고
    • A structural model of the complex formed by phospholamban and the calcium pump of sarcoplasmic reticulum obtained by molecular mechanics
    • Hutter, M. C., Krebs, J., Meiler, J., Griesinger, C., Carafoli, E., and Helms, V. (2002) A structural model of the complex formed by phospholamban and the calcium pump of sarcoplasmic reticulum obtained by molecular mechanics. ChemBioChem 3, 1200-1208.
    • (2002) ChemBioChem , vol.3 , pp. 1200-1208
    • Hutter, M.C.1    Krebs, J.2    Meiler, J.3    Griesinger, C.4    Carafoli, E.5    Helms, V.6
  • 33
    • 0033040491 scopus 로고    scopus 로고
    • Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer
    • Pollesello, P., Annila, A., and Ovaska, M. (1999) Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer. Biophys. J. 76, 1784-1795.
    • (1999) Biophys. J , vol.76 , pp. 1784-1795
    • Pollesello, P.1    Annila, A.2    Ovaska, M.3
  • 34
    • 16344378243 scopus 로고    scopus 로고
    • Mapping the interaction surface of a membrane protein: Unveiling the conformational switch of phospholamban in calcium pump regulation
    • Zamoon, J., Nitu, F., Karim, C., Thomas, D. D., and Veglia, G. (2005) Mapping the interaction surface of a membrane protein: Unveiling the conformational switch of phospholamban in calcium pump regulation. Proc. Natl. Acad. Sci. U.S.A. 102, 4747-4752.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 4747-4752
    • Zamoon, J.1    Nitu, F.2    Karim, C.3    Thomas, D.D.4    Veglia, G.5
  • 38
    • 0015403570 scopus 로고
    • Phospholipid orientation in sarcoplasmic membranes - Spin-label ESR and proton NMR studies
    • Eletr, S., and Inesi, G. (1972) Phospholipid orientation in sarcoplasmic membranes - Spin-label ESR and proton NMR studies. Biochim. Biophys. Acta 282, 174-179.
    • (1972) Biochim. Biophys. Acta , vol.282 , pp. 174-179
    • Eletr, S.1    Inesi, G.2
  • 39
    • 0025019294 scopus 로고
    • Three-dimensional crystals of CaATPase from sarcoplasmic reticulum. Symmetry and molecular packing
    • Stokes, D. L., and Green, N. M. (1990) Three-dimensional crystals of CaATPase from sarcoplasmic reticulum. Symmetry and molecular packing. Biophys. J. 57, 1-14.
    • (1990) Biophys. J , vol.57 , pp. 1-14
    • Stokes, D.L.1    Green, N.M.2
  • 41
    • 0000432697 scopus 로고    scopus 로고
    • Fivefold symmetric homonuclear dipolar recoupling in rotating solids: Application to double quantum spectroscopy
    • Hohwy, M., Rienstra, C. M., Jaroniec, C. P., and Griffin, R. G. (1999) Fivefold symmetric homonuclear dipolar recoupling in rotating solids: Application to double quantum spectroscopy. J. Chem. Phys. 110, 7983-7992.
    • (1999) J. Chem. Phys , vol.110 , pp. 7983-7992
    • Hohwy, M.1    Rienstra, C.M.2    Jaroniec, C.P.3    Griffin, R.G.4
  • 42
    • 0001739017 scopus 로고
    • On the interaction of nuclear spins in a crystalline lattice
    • Bloembergen, N. (1949) On the interaction of nuclear spins in a crystalline lattice. Physica 15, 386-426.
    • (1949) Physica , vol.15 , pp. 386-426
    • Bloembergen, N.1
  • 43
    • 0001437077 scopus 로고
    • Spectral spin diffusion in the presence of an extraneous dipolar reservoir
    • Suter, D., and Ernst, R. R. (1982) Spectral spin diffusion in the presence of an extraneous dipolar reservoir. Phys. Rev. B: Condens. Matter Mater. Phys. 25, 6038-6041.
    • (1982) Phys. Rev. B: Condens. Matter Mater. Phys , vol.25 , pp. 6038-6041
    • Suter, D.1    Ernst, R.R.2
  • 45
    • 0037008857 scopus 로고    scopus 로고
    • Correlation experiments for assignment and structure elucidation of immobilized polypeptides under magic angle spinning
    • Baldus, M. (2002) Correlation experiments for assignment and structure elucidation of immobilized polypeptides under magic angle spinning. Prog. Nucl. Magn. Reson. Spectrosc. 41, 1-47.
    • (2002) Prog. Nucl. Magn. Reson. Spectrosc , vol.41 , pp. 1-47
    • Baldus, M.1
  • 46
    • 0000368822 scopus 로고    scopus 로고
    • Cross polarization in the tilted frame: Assignment and spectral simplification in heteronuclear spin systems
    • Baldus, M., Petkova, A. T., Herzfeld, J., and Griffin, R. G. (1998) Cross polarization in the tilted frame: Assignment and spectral simplification in heteronuclear spin systems. Mol. Phys. 95, 1197-1207.
    • (1998) Mol. Phys , vol.95 , pp. 1197-1207
    • Baldus, M.1    Petkova, A.T.2    Herzfeld, J.3    Griffin, R.G.4
  • 47
    • 0000953276 scopus 로고    scopus 로고
    • 1H dipolar-assisted rotational resonance in magic-angle spinning NMR
    • 1H dipolar-assisted rotational resonance in magic-angle spinning NMR. Chem. Phys. Lett. 344, 631-637.
    • (2001) Chem. Phys. Lett , vol.344 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 48
    • 33845560617 scopus 로고
    • Enhancement of nuclear magnetic resonance signals by polarization transfer
    • Morris, G. A., and Freeman, R. (1979) Enhancement of nuclear magnetic resonance signals by polarization transfer. J. Am. Chem. Soc. 101, 760-762.
    • (1979) J. Am. Chem. Soc , vol.101 , pp. 760-762
    • Morris, G.A.1    Freeman, R.2
  • 49
    • 33646720540 scopus 로고    scopus 로고
    • Total correlation spectroscopy in the solid state. The use of scalar couplings to determine the through-bond connectivity
    • Baldus, M., and Meier, B. H. (1996) Total correlation spectroscopy in the solid state. The use of scalar couplings to determine the through-bond connectivity. J. Magn. Reson. A 121, 65-69.
    • (1996) J. Magn. Reson. A , vol.121 , pp. 65-69
    • Baldus, M.1    Meier, B.H.2
  • 50
    • 0033629304 scopus 로고    scopus 로고
    • An improved broadband decoupling sequence for liquid crystals and solids
    • Fung, B. M., Khitrin, A. K., and Ermolaev, K. (2000) An improved broadband decoupling sequence for liquid crystals and solids. J. Magn. Reson. 142, 97-101.
    • (2000) J. Magn. Reson , vol.142 , pp. 97-101
    • Fung, B.M.1    Khitrin, A.K.2    Ermolaev, K.3
  • 51
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka, A. J., Barker, P. B., and Freeman, R. (1985) Computer-optimized decoupling scheme for wideband applications and low-level operation. J. Magn. Reson. 64, 547-552.
    • (1985) J. Magn. Reson , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 52
    • 0026223896 scopus 로고
    • A relational database for sequence-specific protein NMR data
    • Seavey, B. R., Farr, E. A., Westler, W. M., and Markley, J. L. (1991) A relational database for sequence-specific protein NMR data. J. Biomol. NMR 1, 217-236.
    • (1991) J. Biomol. NMR , vol.1 , pp. 217-236
    • Seavey, B.R.1    Farr, E.A.2    Westler, W.M.3    Markley, J.L.4
  • 54
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez, C., Boelens, R., and Bonvin, A. (2003) HADDOCK: A protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 125, 1731-1737.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.3
  • 56
    • 0036129107 scopus 로고    scopus 로고
    • Probability-based protein secondary structure identification using combined NMR chemical-shift data
    • Wang, Y. J., and Jardetzky, O. (2002) Probability-based protein secondary structure identification using combined NMR chemical-shift data. Protein Sci. 11, 852-861.
    • (2002) Protein Sci , vol.11 , pp. 852-861
    • Wang, Y.J.1    Jardetzky, O.2
  • 57
    • 34347247711 scopus 로고    scopus 로고
    • Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors
    • Takahashi, M., Kondou, Y., and Toyoshima, C. (2007) Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors. Proc. Natl. Acad. Sci. U.S.A. 104, 5800-5805.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 5800-5805
    • Takahashi, M.1    Kondou, Y.2    Toyoshima, C.3


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