메뉴 건너뛰기




Volumn 376, Issue 1, 2008, Pages 35-41

Folding and Assembly of Proteorhodopsin

Author keywords

hexamer; high resolution atomic force microscopy; membrane protein folding; oligomeric state; single molecule force spectroscopy

Indexed keywords

BACTERIORHODOPSIN; HALORHODOPSIN; PROTEORHODOPSIN; RHODOPSIN; UNCLASSIFIED DRUG;

EID: 38049055850     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.11.030     Document Type: Article
Times cited : (89)

References (37)
  • 1
    • 0032144042 scopus 로고    scopus 로고
    • The structure and mechanism of the family of retinal proteins from halophilic archaea
    • Oesterhelt D. The structure and mechanism of the family of retinal proteins from halophilic archaea. Curr. Opin. Struct. Biol. 8 (1998) 489-500
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 489-500
    • Oesterhelt, D.1
  • 2
    • 33645535034 scopus 로고    scopus 로고
    • G protein-coupled receptor rhodopsin
    • Palczewski K. G protein-coupled receptor rhodopsin. Annu. Rev. Biochem. 75 (2006) 743-767
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 743-767
    • Palczewski, K.1
  • 3
    • 0035943457 scopus 로고    scopus 로고
    • Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction
    • Luecke H., Schobert B., Lanyi J.K., Spudich E.N., and Spudich J.L. Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction. Science 293 (2001) 1499-1503
    • (2001) Science , vol.293 , pp. 1499-1503
    • Luecke, H.1    Schobert, B.2    Lanyi, J.K.3    Spudich, E.N.4    Spudich, J.L.5
  • 5
    • 0034665853 scopus 로고    scopus 로고
    • Bacterial rhodopsin: evidence for a new type of phototrophy in the sea
    • Beja O., Aravind L., Koonin E.V., Suzuki M.T., Hadd A., Nguyen L.P., et al. Bacterial rhodopsin: evidence for a new type of phototrophy in the sea. Science 289 (2000) 1902-1906
    • (2000) Science , vol.289 , pp. 1902-1906
    • Beja, O.1    Aravind, L.2    Koonin, E.V.3    Suzuki, M.T.4    Hadd, A.5    Nguyen, L.P.6
  • 10
    • 0038391981 scopus 로고    scopus 로고
    • Diversification and spectral tuning in marine proteorhodopsins
    • Man D., Wang W., Sabehi G., Aravind L., Post A.F., Massana R., et al. Diversification and spectral tuning in marine proteorhodopsins. EMBO J. 22 (2003) 1725-1731
    • (2003) EMBO J. , vol.22 , pp. 1725-1731
    • Man, D.1    Wang, W.2    Sabehi, G.3    Aravind, L.4    Post, A.F.5    Massana, R.6
  • 11
    • 23944505538 scopus 로고    scopus 로고
    • New insights into metabolic properties of marine bacteria encoding proteorhodopsins
    • Sabehi G., Loy A., Jung K.H., Partha R., Spudich J.L., Isaacson T., et al. New insights into metabolic properties of marine bacteria encoding proteorhodopsins. PLoS Biol. 3 (2005) e273
    • (2005) PLoS Biol. , vol.3
    • Sabehi, G.1    Loy, A.2    Jung, K.H.3    Partha, R.4    Spudich, J.L.5    Isaacson, T.6
  • 13
    • 6944240079 scopus 로고    scopus 로고
    • Darwinian adaptation of proteorhodopsin to different light intensities in the marine environment
    • Bielawski J.P., Dunn K.A., Sabehi G., and Beja O. Darwinian adaptation of proteorhodopsin to different light intensities in the marine environment. Proc. Natl Acad. Sci. USA 101 (2004) 14824-14829
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 14824-14829
    • Bielawski, J.P.1    Dunn, K.A.2    Sabehi, G.3    Beja, O.4
  • 15
    • 32844465575 scopus 로고    scopus 로고
    • Proteorhodopsin lateral gene transfer between marine planktonic Bacteria and Archaea
    • Frigaard N.U., Martinez A., Mincer T.J., and DeLong E.F. Proteorhodopsin lateral gene transfer between marine planktonic Bacteria and Archaea. Nature 439 (2006) 847-850
    • (2006) Nature , vol.439 , pp. 847-850
    • Frigaard, N.U.1    Martinez, A.2    Mincer, T.J.3    DeLong, E.F.4
  • 18
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution
    • Kolbe M., Besir H., Essen L.O., and Oesterhelt D. Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution. Science 288 (2000) 1390-1396
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 21
    • 34347218989 scopus 로고    scopus 로고
    • The directed cooperative assembly of proteorhodopsin into 2D and 3D polarized arrays
    • Liang H., Whited G., Nguyen C., and Stucky G.D. The directed cooperative assembly of proteorhodopsin into 2D and 3D polarized arrays. Proc. Natl Acad. Sci. USA 104 (2007) 8212-8217
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 8212-8217
    • Liang, H.1    Whited, G.2    Nguyen, C.3    Stucky, G.D.4
  • 22
    • 36849012989 scopus 로고    scopus 로고
    • Proteorhodopsin: characterisation of 2D crystals by electron microscopy and solid state NMR
    • 10.1096/10.1016/j.bbamem.2007.10.001 in press
    • Shastri S., Vonck J., Pfleger N., Haase W., Kuehlbrandt W., and Glaubitz C. Proteorhodopsin: characterisation of 2D crystals by electron microscopy and solid state NMR. BBA Biomembranes (2007) 10.1096/10.1016/j.bbamem.2007.10.001 in press
    • (2007) BBA Biomembranes
    • Shastri, S.1    Vonck, J.2    Pfleger, N.3    Haase, W.4    Kuehlbrandt, W.5    Glaubitz, C.6
  • 23
    • 37849010835 scopus 로고    scopus 로고
    • Characterisation of Schiff base and chromophore in green proteorhodopsin by solid-state NMR
    • 10.1007/s10858-007-9203-5
    • Pfleger N., Lorch M., Woerner A., Shastri S., and Glaubitz C. Characterisation of Schiff base and chromophore in green proteorhodopsin by solid-state NMR. J. Biomol. NMR (2007) 10.1007/s10858-007-9203-5
    • (2007) J. Biomol. NMR
    • Pfleger, N.1    Lorch, M.2    Woerner, A.3    Shastri, S.4    Glaubitz, C.5
  • 25
    • 0040298977 scopus 로고    scopus 로고
    • Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane
    • Müller D.J., Sass H.-J., Müller S., Büldt G., and Engel A. Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane. J. Mol. Biol. 285 (1999) 1903-1909
    • (1999) J. Mol. Biol. , vol.285 , pp. 1903-1909
    • Müller, D.J.1    Sass, H.-J.2    Müller, S.3    Büldt, G.4    Engel, A.5
  • 27
    • 13844298943 scopus 로고    scopus 로고
    • Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin
    • Cisneros D.A., Oesterhelt D., and Muller D.J. Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin. Structure 13 (2005) 235-242
    • (2005) Structure , vol.13 , pp. 235-242
    • Cisneros, D.A.1    Oesterhelt, D.2    Muller, D.J.3
  • 28
    • 34347259478 scopus 로고    scopus 로고
    • Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy
    • Kedrov A., Janovjak H., Sapra K.T., and Muller D.J. Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy. Annu. Rev. Biophys. Biomol. Struct. 36 (2007) 233-260
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 233-260
    • Kedrov, A.1    Janovjak, H.2    Sapra, K.T.3    Muller, D.J.4
  • 29
    • 0036932510 scopus 로고    scopus 로고
    • Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy
    • Müller D.J., Kessler M., Oesterhelt F., Moeller C., Oesterhelt D., and Gaub H. Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy. Biophys. J. 83 (2002) 3578-3588
    • (2002) Biophys. J. , vol.83 , pp. 3578-3588
    • Müller, D.J.1    Kessler, M.2    Oesterhelt, F.3    Moeller, C.4    Oesterhelt, D.5    Gaub, H.6
  • 32
    • 23844528739 scopus 로고    scopus 로고
    • Formation of a long-lived photoproduct with a deprotonated Schiff base in proteorhodopsin, and its enhancement by mutation of Asp227
    • Imasheva E.S., Shimono K., Balashov S.P., Wang J.M., Zadok U., Sheves M., et al. Formation of a long-lived photoproduct with a deprotonated Schiff base in proteorhodopsin, and its enhancement by mutation of Asp227. Biochemistry 44 (2005) 10828-10838
    • (2005) Biochemistry , vol.44 , pp. 10828-10838
    • Imasheva, E.S.1    Shimono, K.2    Balashov, S.P.3    Wang, J.M.4    Zadok, U.5    Sheves, M.6
  • 34
    • 29144532994 scopus 로고    scopus 로고
    • Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy
    • Sapra K.T., Besir H., Oesterhelt D., and Muller D.J. Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy. J. Mol. Biol. 355 (2006) 640-650
    • (2006) J. Mol. Biol. , vol.355 , pp. 640-650
    • Sapra, K.T.1    Besir, H.2    Oesterhelt, D.3    Muller, D.J.4
  • 35
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • Engelman D.M. Membranes are more mosaic than fluid. Nature 438 (2005) 578-580
    • (2005) Nature , vol.438 , pp. 578-580
    • Engelman, D.M.1
  • 36
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • Müller D.J., Amrein M., and Engel A. Adsorption of biological molecules to a solid support for scanning probe microscopy. J. Struct. Biol. 119 (1997) 172-188
    • (1997) J. Struct. Biol. , vol.119 , pp. 172-188
    • Müller, D.J.1    Amrein, M.2    Engel, A.3
  • 37
    • 0039114981 scopus 로고    scopus 로고
    • Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscopy
    • Müller D.J., Fotiadis D., Scheuring S., Müller S.A., and Engel A. Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscopy. Biophys. J. 76 (1999) 1101-1111
    • (1999) Biophys. J. , vol.76 , pp. 1101-1111
    • Müller, D.J.1    Fotiadis, D.2    Scheuring, S.3    Müller, S.A.4    Engel, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.