메뉴 건너뛰기




Volumn 91, Issue 2, 1997, Pages 263-270

Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONIN;

EID: 0030668929     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80408-0     Document Type: Article
Times cited : (141)

References (45)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J.P., and Leslie, A.G.W. (1996). Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D 52, 30-42.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 2
    • 0030031369 scopus 로고    scopus 로고
    • Purification and structural characterization of the thermosome from the hyperthermophilic archaeum Methanopyruskandleri
    • Andrä, S., Frey, G., Nitsch, M., Baumeister, W., and Stetter, K.O. (1996). Purification and structural characterization of the thermosome from the hyperthermophilic archaeum Methanopyruskandleri. FEBS Lett. 379, 127-131.
    • (1996) FEBS Lett. , vol.379 , pp. 127-131
    • Andrä, S.1    Frey, G.2    Nitsch, M.3    Baumeister, W.4    Stetter, K.O.5
  • 3
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin groEL at 2.8 Å resolution
    • Braig, K., Adams, P.D., and Brünger, A.T. (1995). Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nature Struct. Biol. 2, 1083-1094.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brünger, A.T.3
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 7
    • 0029769797 scopus 로고    scopus 로고
    • Newly synthesized β-Tubulin demonstrates domain-specific interactions with the cytosolic chaperonin
    • Dobrzynski, J.K., Sternlicht, M.L., Farr, G.W., and Sternlicht, H. (1996). Newly synthesized β-Tubulin demonstrates domain-specific interactions with the cytosolic chaperonin. Biochemistry 35, 15870-15882.
    • (1996) Biochemistry , vol.35 , pp. 15870-15882
    • Dobrzynski, J.K.1    Sternlicht, M.L.2    Farr, G.W.3    Sternlicht, H.4
  • 8
    • 0026755556 scopus 로고
    • Cytosolic chaperonin confirmed
    • Ellis, R.J. (1992). Cytosolic chaperonin confirmed. Nature 358, 191-192.
    • (1992) Nature , vol.358 , pp. 191-192
    • Ellis, R.J.1
  • 9
    • 0004167360 scopus 로고    scopus 로고
    • San Diego, CA: Academic Press
    • Ellis, R.J. (1996).The Chaperonins (San Diego, CA: Academic Press).
    • (1996) The Chaperonins
    • Ellis, R.J.1
  • 10
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A., and Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A 47, 392-400.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 11
    • 0030910349 scopus 로고    scopus 로고
    • Groel-mediated protein folding
    • Fenton, W.A., and Horwich, A.L. (1997). Groel-mediated protein folding. Protein Sci. 6, 743-760.
    • (1997) Protein Sci. , vol.6 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 12
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton, W.A., Kashi, Y., Furtak, K., and Horwich, A.L. (1994). Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371, 614-619.
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 13
    • 0027077442 scopus 로고
    • Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
    • Frydman, J., Nimmesgern, E., Erdjument-Bromage, H., Wall, J.S., Tempst, P., and Hartl, F.-U. (1992). Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J. 11, 4767-4778.
    • (1992) EMBO J. , vol.11 , pp. 4767-4778
    • Frydman, J.1    Nimmesgern, E.2    Erdjument-Bromage, H.3    Wall, J.S.4    Tempst, P.5    Hartl, F.-U.6
  • 14
    • 0026776331 scopus 로고
    • A cytoplasmatic chaperonin that catalyzes β-Actin folding
    • Gao, Y., Thomas, J.O., Chow, R.L., Lee, G.H., and Cowan, N.J. (1992). A cytoplasmatic chaperonin that catalyzes β-Actin folding. Cell 69, 1043-1050.
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 15
    • 0028019612 scopus 로고
    • The chaperonin from the archaeon Sulfolobussolfataricus promotes correct refolding and prevents thermal denaturation in vitro
    • Guagliardi, A., Cerchia, L., Bartolucci, S., and Rossi, M. (1994). The chaperonin from the archaeon Sulfolobussolfataricus promotes correct refolding and prevents thermal denaturation in vitro. Protein Sci. 3, 1436-1443.
    • (1994) Protein Sci. , vol.3 , pp. 1436-1443
    • Guagliardi, A.1    Cerchia, L.2    Bartolucci, S.3    Rossi, M.4
  • 16
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 17
    • 0029879294 scopus 로고    scopus 로고
    • The EM program package: A platform for image processing in biological electron microscopy
    • Hegerl, R. (1996). The EM program package: a platform for image processing in biological electron microscopy. J. Struct. Biol. 116, 30-34.
    • (1996) J. Struct. Biol. , vol.116 , pp. 30-34
    • Hegerl, R.1
  • 18
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES cochaperonin at 2.8 Å resolution
    • Hunt, J.F., Weaver, A.J., Landry, S.J., Gierasch, L., and Deisenhofer, J. (1996). The crystal structure of the GroES cochaperonin at 2.8 Å resolution. Nature 379, 37-45.
    • (1996) Nature , vol.379 , pp. 37-45
    • Hunt, J.F.1    Weaver, A.J.2    Landry, S.J.3    Gierasch, L.4    Deisenhofer, J.5
  • 19
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., and Cowan, S.W. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3
  • 20
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 21
    • 0027992757 scopus 로고
    • Cytosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide binding domains
    • Kim, S., Willison, K.R., and Horwich, A.L. (1994). Cytosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide binding domains. Trends Biochem. Sci 19, 543-548.
    • (1994) Trends Biochem. Sci , vol.19 , pp. 543-548
    • Kim, S.1    Willison, K.R.2    Horwich, A.L.3
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0028938750 scopus 로고
    • The eighth Cct gene, Cctq, encoding the theta subunit of the cytosolic chaperonin containing TCP-1
    • Kubota, H., Hynes, G., and Willison, K. (1995). The eighth Cct gene, Cctq, encoding the theta subunit of the cytosolic chaperonin containing TCP-1. Gene 154, 231-236.
    • (1995) Gene , vol.154 , pp. 231-236
    • Kubota, H.1    Hynes, G.2    Willison, K.3
  • 24
    • 0027092285 scopus 로고
    • Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity
    • Langer, T., Pfeifer, G., Martin, J., Baumeister, W., and Hartl, F.U. (1992). Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J. 11, 4757-4765.
    • (1992) EMBO J. , vol.11 , pp. 4757-4765
    • Langer, T.1    Pfeifer, G.2    Martin, J.3    Baumeister, W.4    Hartl, F.U.5
  • 25
    • 0026683609 scopus 로고
    • T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cystosol
    • Lewis, VA, Hynes, G.M., Zheng, D., Saibil, H., and Willison, K. (1992). T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cystosol. Nature 358, 249-252.
    • (1992) Nature , vol.358 , pp. 249-252
    • Lewis, V.A.1    Hynes, G.M.2    Zheng, D.3    Saibil, H.4    Willison, K.5
  • 26
    • 0030024540 scopus 로고    scopus 로고
    • Structure of the heat shock protein Chaperonin-10 of Mycobacterium leprae
    • Mande, S.C., Mehra, V., Bloom, B.R., and Hol, W.G.J. (1996). Structure of the heat shock protein Chaperonin-10 of Mycobacterium leprae. Science 271, 203-207.
    • (1996) Science , vol.271 , pp. 203-207
    • Mande, S.C.1    Mehra, V.2    Bloom, B.R.3    Hol, W.G.J.4
  • 27
    • 0028180775 scopus 로고
    • Reversible interaction of β-actin along the channel of the TCP-1 cytoplasmic chaperonin
    • Marco, S., Carrascosa, J.L., and Valpuesta, J.M. (1994). Reversible interaction of β-actin along the channel of the TCP-1 cytoplasmic chaperonin. Biophys. J. 67, 364-368.
    • (1994) Biophys. J. , vol.67 , pp. 364-368
    • Marco, S.1    Carrascosa, J.L.2    Valpuesta, J.M.3
  • 28
    • 0028173886 scopus 로고
    • Protein structure comparisons using a combination of a genetic algorithm, dynamic programming, and least-squares minimization
    • May, A.C.W., and Johnson, M.S. (1994). Protein structure comparisons using a combination of a genetic algorithm, dynamic programming, and least-squares minimization. Protein Eng. 7, 475-485.
    • (1994) Protein Eng. , vol.7 , pp. 475-485
    • May, A.C.W.1    Johnson, M.S.2
  • 29
    • 0343907201 scopus 로고    scopus 로고
    • Cytoplasmic chaperonin containing tcp-1 - Structural and functional-characterization
    • Melki, R., Batelier, G., Soulie, S., and Williams, R.C. (1997). Cytoplasmic chaperonin containing tcp-1 - structural and functional-characterization. Biochemistry 36, 5817-5826.
    • (1997) Biochemistry , vol.36 , pp. 5817-5826
    • Melki, R.1    Batelier, G.2    Soulie, S.3    Williams, R.C.4
  • 30
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt, E.A., and Murphy, M.E.P. (1994). Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D 50, 869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 32
    • 0031582064 scopus 로고    scopus 로고
    • The thermosome - Alternating α and β subunits within the chaperonin of the archaeon Thermoplasma acidophilum
    • Nitsch, M., Klumpp, M., Lupas, A., and Baumeister, W. (1997). The thermosome - alternating α and β subunits within the chaperonin of the archaeon Thermoplasma acidophilum. J. Mol. Biol. 267, 142-149.
    • (1997) J. Mol. Biol. , vol.267 , pp. 142-149
    • Nitsch, M.1    Klumpp, M.2    Lupas, A.3    Baumeister, W.4
  • 33
    • 0025892424 scopus 로고
    • A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria
    • Phipps, B.M., Hoffmann, A., Stetter, K.O., and Baumeister, W. (1991). A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria. EMBO J. 10, 1711-1722.
    • (1991) EMBO J. , vol.10 , pp. 1711-1722
    • Phipps, B.M.1    Hoffmann, A.2    Stetter, K.O.3    Baumeister, W.4
  • 35
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman, A.M., Chen, S.X., White, H., Braig, K., and Saibil, H.R. (1996). The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell 87, 241-251.
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.X.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 37
    • 0026416668 scopus 로고
    • Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects
    • Sharp, K.A., Nicholls, A., Friedman, R., and Honig, B. (1991). Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects. Science 252, 106-109.
    • (1991) Science , vol.252 , pp. 106-109
    • Sharp, K.A.1    Nicholls, A.2    Friedman, R.3    Honig, B.4
  • 38
    • 0025748752 scopus 로고
    • A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
    • Trent, J.D., Nimmesgern, E., Wall, J.S., Hartl, F.U., and Horwich, A.L. (1991 ). A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 354, 490-493.
    • (1991) Nature , vol.354 , pp. 490-493
    • Trent, J.D.1    Nimmesgern, E.2    Wall, J.S.3    Hartl, F.U.4    Horwich, A.L.5
  • 41
    • 0028791460 scopus 로고
    • Expression of an archaeal chaperonin in E. coli: Formation of homo-(α,β) and heterooligomeric (α+β) thermosome complexes
    • Waldmann, T., Nitsch, M., Klumpp, M., and Baumeister, W. (1995c). Expression of an archaeal chaperonin in E. coli: formation of homo-(α,β) and heterooligomeric (α+β) thermosome complexes. FEBS Lett. 376, 67-73.
    • (1995) FEBS Lett. , vol.376 , pp. 67-73
    • Waldmann, T.1    Nitsch, M.2    Klumpp, M.3    Baumeister, W.4
  • 42
    • 0001314116 scopus 로고    scopus 로고
    • Structure and function of chaperonins in archaebacteria and eukaryotic cytosol
    • R.J. Ellis, ed. (San Diego, CA: Academic Press)
    • Willison, K.R., and Horwich, A.L. (1996). Structure and function of chaperonins in archaebacteria and eukaryotic cytosol. In The Chaperonins, R.J. Ellis, ed. (San Diego, CA: Academic Press), pp. 107-136.
    • (1996) The Chaperonins , pp. 107-136
    • Willison, K.R.1    Horwich, A.L.2
  • 43
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP), chaperonin complex
    • Xu, Z., Horwich, A.L., and Sigler, P.B. (1997). The crystal structure of the asymmetric GroEL-GroES-(ADP), chaperonin complex. Nature 388, 741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.