메뉴 건너뛰기




Volumn 7, Issue 4, 1997, Pages 550-556

Keeping calcium in its place: Ca2+-ATPase and phospholamban

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); PHOSPHOLAMBAN;

EID: 0030841626     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80121-2     Document Type: Article
Times cited : (33)

References (27)
  • 2
    • 0021930155 scopus 로고
    • Dimer ribbons in the three-dimensional structure of sarcoplasmic reticulum
    • Castellani L, Hardwicke PM, Vibert P. Dimer ribbons in the three-dimensional structure of sarcoplasmic reticulum. J Mol Biol. 185:1985;579-594.
    • (1985) J Mol Biol , vol.185 , pp. 579-594
    • Castellani, L.1    Hardwicke, P.M.2    Vibert, P.3
  • 3
    • 0027512587 scopus 로고
    • Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane
    • Toyoshima C, Sasabe H, Stokes DL. Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane. Nature. 362:1993;469-471.
    • (1993) Nature , vol.362 , pp. 469-471
    • Toyoshima, C.1    Sasabe, H.2    Stokes, D.L.3
  • 4
    • 0031041716 scopus 로고    scopus 로고
    • 2+-ATPase revealed by electron image analysis
    • of outstanding interest. Difference maps are calculated between crystalline tubes with and without Cr-ATP. The statistical significance of the difference density is verified with a Student's T-test. This provides an important verification of an earlier hypothesis for the physical location of the ATP-binding site on the molecule and represents the first link between the 14 Å resolution structure and the amino acid sequence.
    • 2+-ATPase revealed by electron image analysis. of outstanding interest Biophys J. 72:1997;997-1005 Difference maps are calculated between crystalline tubes with and without Cr-ATP. The statistical significance of the difference density is verified with a Student's T-test. This provides an important verification of an earlier hypothesis for the physical location of the ATP-binding site on the molecule and represents the first link between the 14 Å resolution structure and the amino acid sequence.
    • (1997) Biophys J , vol.72 , pp. 997-1005
    • Yonekura, K.1    Stokes, D.L.2    Sasabe, H.3    Toyoshima, C.4
  • 5
    • 0028236332 scopus 로고
    • Structure, transmembrane topology and helix packing of P-type ion pumps
    • Stokes DL, Taylor WR, Green NM. Structure, transmembrane topology and helix packing of P-type ion pumps. FEBS Lett. 346:1994;32-38.
    • (1994) FEBS Lett , vol.346 , pp. 32-38
    • Stokes, D.L.1    Taylor, W.R.2    Green, N.M.3
  • 6
    • 0022371456 scopus 로고
    • 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence
    • 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature. 316:1985;696-700.
    • (1985) Nature , vol.316 , pp. 696-700
    • MacLennan, D.H.1    Brandl, C.J.2    Korczak, B.3    Green, N.M.4
  • 7
    • 0001791586 scopus 로고
    • Crystallization of membrane proteins
    • Michel H. Crystallization of membrane proteins. Trends Biochem Sci. 8:1983;56-59.
    • (1983) Trends Biochem Sci , vol.8 , pp. 56-59
    • Michel, H.1
  • 8
    • 0025344903 scopus 로고
    • Structure of CaATPase: Electron microscopy of frozen-hydrated crystals at 6 Å resolution in projection
    • Stokes DL, Green NM. Structure of CaATPase: electron microscopy of frozen-hydrated crystals at 6 Å resolution in projection. J Mol Biol. 213:1990;529-538.
    • (1990) J Mol Biol , vol.213 , pp. 529-538
    • Stokes, D.L.1    Green, N.M.2
  • 9
    • 0029994944 scopus 로고    scopus 로고
    • 2+-ATPase from sarcoplasmic reticulum
    • 2+-ATPase in this crystal form with that from crystalline tubes, revealing the nature of the conformational change that occurs upon calcium binding.
    • 2+-ATPase in this crystal form with that from crystalline tubes, revealing the nature of the conformational change that occurs upon calcium binding.
    • (1996) Biophys J , vol.70 , pp. 1689-1699
    • Cheong, G.-W.1    Young, H.S.2    Ogawa, H.3    Toyoshima, C.4    Stokes, D.L.5
  • 10
    • 0025019294 scopus 로고
    • Three-dimensional crystals of Ca-ATPase from sarcoplasmic reticulum: Symmetry and molecular packing
    • Stokes DL, Green NM. Three-dimensional crystals of Ca-ATPase from sarcoplasmic reticulum: symmetry and molecular packing. Biophys J. 57:1990;1-14.
    • (1990) Biophys J , vol.57 , pp. 1-14
    • Stokes, D.L.1    Green, N.M.2
  • 12
    • 0028179410 scopus 로고
    • 2+, thapsigargin, AMP-PCP, and Cr-ATP on crystallization
    • 2+, thapsigargin, AMP-PCP, and Cr-ATP on crystallization. J Biol Chem. 269:1994;11606-11613.
    • (1994) J Biol Chem , vol.269 , pp. 11606-11613
    • Stokes, D.L.1    Lacapere, J.-J.2
  • 14
    • 0028569793 scopus 로고
    • Applications of a slow-scan CCD camera in protein electron crystallography
    • Brink J, Chiu W. Applications of a slow-scan CCD camera in protein electron crystallography. J Struct Biol. 113:1994;23-34.
    • (1994) J Struct Biol , vol.113 , pp. 23-34
    • Brink, J.1    Chiu, W.2
  • 15
    • 0028950657 scopus 로고
    • Secondary structure and orientation of phospholamban reconstituted in supported bilayers from polarized attenuated total reflection FTIR spectroscopy
    • Tatulian SA, Jones LR, Reddy LG, Stokes DL, Tamm LK. Secondary structure and orientation of phospholamban reconstituted in supported bilayers from polarized attenuated total reflection FTIR spectroscopy. Biochemistry. 34:1995;4448-4456.
    • (1995) Biochemistry , vol.34 , pp. 4448-4456
    • Tatulian, S.A.1    Jones, L.R.2    Reddy, L.G.3    Stokes, D.L.4    Tamm, L.K.5
  • 17
    • 0028999102 scopus 로고
    • Solution structure of the cytoplasmic domain of phospholamban: Phosphorylation leads to a local perturbation of secondary structure
    • Mortishire-Smith RJ, Pitzenberger SM, Burke CJ, Middaugh CR, Garsky VM, Johnson RG. Solution structure of the cytoplasmic domain of phospholamban: phosphorylation leads to a local perturbation of secondary structure. Biochemistry. 34:1995;7603-7613.
    • (1995) Biochemistry , vol.34 , pp. 7603-7613
    • Mortishire-Smith, R.J.1    Pitzenberger, S.M.2    Burke, C.J.3    Middaugh, C.R.4    Garsky, V.M.5    Johnson, R.G.6
  • 19
    • 0028063482 scopus 로고
    • Structural organization of the pentameric transmembrane a-helices of phospholamban, a cardiac ion channel
    • Arkin IT, Adams PD, Mackenzie KR, Lemmon MA, Brunger AT, Engelman DM. Structural organization of the pentameric transmembrane a-helices of phospholamban, a cardiac ion channel. EMBO J. 13:1994;4757-4764.
    • (1994) EMBO J , vol.13 , pp. 4757-4764
    • Arkin, I.T.1    Adams, P.D.2    Mackenzie, K.R.3    Lemmon, M.A.4    Brunger, A.T.5    Engelman, D.M.6
  • 20
    • 0029557910 scopus 로고
    • Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
    • Adams PD, Arkin IT, Engleman DM, Brunger AT. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Nat Struct Biol. 2:1995;154-162.
    • (1995) Nat Struct Biol , vol.2 , pp. 154-162
    • Adams, P.D.1    Arkin, I.T.2    Engleman, D.M.3    Brunger, A.T.4
  • 21
    • 0029862745 scopus 로고    scopus 로고
    • A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure
    • of special interest, of outstanding interest. Another study of pentamer stability by mutagenesis of the transmembrane domain. Full-length PLB is expressed, in this case, and the pattern of disruptive residues is similar to that of Arkin et al. [19]. The archetypic leucine zipper is used as a basis for the model of a five-stranded coiled coil. As a result, the rotational orientation of helices within the coiled coil are different than those of Adams et al. [20] by 45° but consistent with the X-ray structure of a structurally related coiled coil by Malashkevich et al. [23].
    • Simmerman HKB, Kobayashi YM, Autry JM, Jones LR. A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure. of special interest, of outstanding interest J Biol Chem. 271:1996;5941-5946 Another study of pentamer stability by mutagenesis of the transmembrane domain. Full-length PLB is expressed, in this case, and the pattern of disruptive residues is similar to that of Arkin et al. [19]. The archetypic leucine zipper is used as a basis for the model of a five-stranded coiled coil. As a result, the rotational orientation of helices within the coiled coil are different than those of Adams et al. [20] by 45° but consistent with the X-ray structure of a structurally related coiled coil by Malashkevich et al. [23].
    • (1996) J Biol Chem , vol.271 , pp. 5941-5946
    • Simmerman, H.K.B.1    Kobayashi, Y.M.2    Autry, J.M.3    Jones, L.R.4
  • 22
    • 0025272940 scopus 로고
    • Alpha-helical coiled coils and bundles: How to design an alpha-helical protein
    • Cohen C, Parry DAD. Alpha-helical coiled coils and bundles: how to design an alpha-helical protein. Proteins. 7:1990;1-15.
    • (1990) Proteins , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 23
    • 0029911261 scopus 로고    scopus 로고
    • The crystal structure of a five-stranded coiled coil in COMP: A prototype ion channel?
    • of special interest. COMP is functionally unrelated to PLB but forms a five-stranded coiled coil and shows exactly the same pattern of leucine and isoleucine residues that stabilize the PLB pentamer. Thus, this structure is likely to be close to that of the transmembrane domain of PLB.
    • Malashkevich VN, Kammerer RA, Efimov VP, Schulthess T, Engel J. The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel? of special interest Science. 274:1996;761-765 COMP is functionally unrelated to PLB but forms a five-stranded coiled coil and shows exactly the same pattern of leucine and isoleucine residues that stabilize the PLB pentamer. Thus, this structure is likely to be close to that of the transmembrane domain of PLB.
    • (1996) Science , vol.274 , pp. 761-765
    • Malashkevich, V.N.1    Kammerer, R.A.2    Efimov, V.P.3    Schulthess, T.4    Engel, J.5
  • 24
    • 0030978470 scopus 로고    scopus 로고
    • Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers
    • of special interest. This first study of the oligomeric state of PLB in the membrane. EPR is used to identify a population of less mobile lipids, which are considered to be boundary lipids. On the basis of geometrical considerations, the ratio of boundary lipids to bulk lipids is then used to estimate the oligomeric state of PLB. Consistent with results from SDS-PAGE, wild-type PLB is found to be oligomeric, albeit with only 3.5 monomers per oligomer, and the mutant Leu37→Ala is monomeric. Interestingly, phosphorylation drives both of these PLBs to a higher oligomeric state (the wild-type to a pentamer and the Leu37→Ala mutant to a dimer).
    • Cornea RL, Jones LR, Autry JM, Thomas DD. Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers. of special interest Biophys J. 36:1997;2960-2967 This first study of the oligomeric state of PLB in the membrane. EPR is used to identify a population of less mobile lipids, which are considered to be boundary lipids. On the basis of geometrical considerations, the ratio of boundary lipids to bulk lipids is then used to estimate the oligomeric state of PLB. Consistent with results from SDS-PAGE, wild-type PLB is found to be oligomeric, albeit with only 3.5 monomers per oligomer, and the mutant Leu37→Ala is monomeric. Interestingly, phosphorylation drives both of these PLBs to a higher oligomeric state (the wild-type to a pentamer and the Leu37→Ala mutant to a dimer).
    • (1997) Biophys J , vol.36 , pp. 2960-2967
    • Cornea, R.L.1    Jones, L.R.2    Autry, J.M.3    Thomas, D.D.4
  • 26
    • 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. 269:1994;22929-22932.
    • (1994) J Biol Chem , vol.269 , pp. 22929-22932
    • Toyofuku, T.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.