메뉴 건너뛰기




Volumn 3, Issue 6, 2004, Pages 543-547

Sensory rhodopsin II and bacteriorhodopsin: Light activated helix F movement

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; MEMBRANE PROTEIN; SENSORY RHODOPSIN;

EID: 3242804523     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/b402656j     Document Type: Article
Times cited : (54)

References (42)
  • 1
    • 0032987196 scopus 로고    scopus 로고
    • General concept for ion translocation by halobacterial retinal proteins – the isomerization/switch/transfer (IST) model
    • U. Haupts J. Tittor D. Oesterhelt General concept for ion translocation by halobacterial retinal proteins – the isomerization/switch/transfer (IST) model Annu. Rev. Biophys. Biomol. Struct. 1999 28 367-399.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 367-399
    • Haupts, U.1    Tittor, J.2    Oesterhelt, D.3
  • 3
    • 0242405537 scopus 로고    scopus 로고
    • Structural and mechanistic insight from high resolution structures of archaeal rhodopsins
    • E. M. Landau E. Pebay-Peyroula R. Neutze Structural and mechanistic insight from high resolution structures of archaeal rhodopsins FEBS Lett. 2003 555 51-56.
    • (2003) FEBS Lett. , vol.555 , pp. 51-56
    • Landau, E.M.1    Pebay-Peyroula, E.2    Neutze, R.3
  • 5
    • 0036667744 scopus 로고    scopus 로고
    • Sensory rhodopsin II: Functional insights from structure
    • J. L. Spudich H. Luecke Sensory rhodopsin II: functional insights from structure Curr. Opin. Struct. Biol. 2002 12 540-546.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 540-546
    • Spudich, J.L.1    Luecke, H.2
  • 6
    • 0141592427 scopus 로고    scopus 로고
    • Conformational changes detected in a sensory rhodopsin II–transducer complex
    • V. Bergo E. N. Spudich J. L. Spudich K. J. Rothschild Conformational changes detected in a sensory rhodopsin II–transducer complex J. Biol. Chem. 2003 278 36556-36562.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36556-36562
    • Bergo, V.1    Spudich, E.N.2    Spudich, J.L.3    Rothschild, K.J.4
  • 7
    • 0036927590 scopus 로고    scopus 로고
    • FTIR spectroscopy of the M photointermediate in pharaonis phoborhodopsin
    • Y. Furutani M. Iwamoto K. Shimono N. Kamo H. Kandori FTIR spectroscopy of the M photointermediate in pharaonis phoborhodopsin Biophys. J. 2002 83 3482-3489.
    • (2002) Biophys. J. , vol.83 , pp. 3482-3489
    • Furutani, Y.1    Iwamoto, M.2    Shimono, K.3    Kamo, N.4    Kandori, H.5
  • 8
    • 0037847498 scopus 로고    scopus 로고
    • FTIR spectroscopy of the complex between pharaonis phoborhodopsin and its transducer protein
    • Y. Furutani Y. Sudo N. Kamo H. Kandori FTIR spectroscopy of the complex between pharaonis phoborhodopsin and its transducer protein Biochemistry 2003 42 4837-4842.
    • (2003) Biochemistry , vol.42 , pp. 4837-4842
    • Furutani, Y.1    Sudo, Y.2    Kamo, N.3    Kandori, H.4
  • 9
    • 0942268923 scopus 로고    scopus 로고
    • Consequences of counterion mutation in sensory rhodopsin II of Natronobacterium pharaonis for photoreaction and receptor activation: An FTIR study
    • M. Hein I. Radu J. P. Klare M. Engelhard F. Siebert Consequences of counterion mutation in sensory rhodopsin II of Natronobacterium pharaonis for photoreaction and receptor activation: An FTIR study Biochemistry 2004 43 995-1002.
    • (2004) Biochemistry , vol.43 , pp. 995-1002
    • Hein, M.1    Radu, I.2    Klare, J.P.3    Engelhard, M.4    Siebert, F.5
  • 10
    • 0037306105 scopus 로고    scopus 로고
    • Time-resolved FTIR studies of sensory rhodopsin II (NpSRII) from Natronobacterium pharaonis: Implications for proton transport and receptor activation
    • M. Hein A. A. Wegener M. Engelhard F. Siebert Time-resolved FTIR studies of sensory rhodopsin II (NpSRII) from Natronobacterium pharaonis: Implications for proton transport and receptor activation Biophys. J. 2003 84 1208-1217.
    • (2003) Biophys. J. , vol.84 , pp. 1208-1217
    • Hein, M.1    Wegener, A.A.2    Engelhard, M.3    Siebert, F.4
  • 12
    • 0037005737 scopus 로고    scopus 로고
    • Association of pharaonis phoborhodopsin with its cognate transducer decreases the photo-dependent reactivity by water-soluble reagents of azide and hydroxylamineyw
    • Y. Sudo M. Iwamoto K. Shimono N. Kamo Association of pharaonis phoborhodopsin with its cognate transducer decreases the photo-dependent reactivity by water-soluble reagents of azide and hydroxylamineyw Biochim. Biophys. Acta – Biomembranes 2002 1558 63-69.
    • (2002) Biochim. Biophys. Acta – Biomembranes , vol.1558 , pp. 63-69
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Kamo, N.4
  • 13
    • 0036283968 scopus 로고    scopus 로고
    • Tyr-199 and charged residues of pharaonis phoborhodopsin are important for the Interaction with its transducer
    • Y. Sudo M. Iwamoto K. Shimono N. Kamo Tyr-199 and charged residues of pharaonis phoborhodopsin are important for the Interaction with its transducer Biophys. J. 2002 83 427-432.
    • (2002) Biophys. J. , vol.83 , pp. 427-432
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Kamo, N.4
  • 14
    • 0035142193 scopus 로고    scopus 로고
    • Photo-induced proton transport of pharaonis phoborhodopsin (Sensory rhodopsin II) is ceased by association with the transducer
    • Y. Sudo M. Iwamoto K. Shimono M. Sumi N. Kamo Photo-induced proton transport of pharaonis phoborhodopsin (sensory rhodopsin II) is ceased by association with the transducer Biophys. J. 2001 80 916-922.
    • (2001) Biophys. J. , vol.80 , pp. 916-922
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Sumi, M.4    Kamo, N.5
  • 15
    • 0344412959 scopus 로고    scopus 로고
    • Photostimulation of a sensory rhodopsin II/HtrII/Tsr fusion chimera activates CheA-autophosphorylation and CheY-phosphotransfer in vitro
    • V. D. Trivedi J. L. Spudich Photostimulation of a sensory rhodopsin II/HtrII/Tsr fusion chimera activates CheA-autophosphorylation and CheY-phosphotransfer in vitro Biochemistry 2003 42 13887-13892.
    • (2003) Biochemistry , vol.42 , pp. 13887-13892
    • Trivedi, V.D.1    Spudich, J.L.2
  • 16
    • 0034714097 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II
    • A. A. Wegener I. Chizhov M. Engelhard H.-J. Steinhoff Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II J. Mol. Biol. 2000 301 881-891.
    • (2000) J. Mol. Biol. , vol.301 , pp. 881-891
    • Wegener, A.A.1    Chizhov, I.2    Engelhard, M.3    Steinhoff, H.-J.4
  • 17
    • 0035477798 scopus 로고    scopus 로고
    • Structural insights into the early steps of receptor–transducer signal transfer in archaeal phototaxis
    • A. A. Wegener J. P. Klare M. Engelhard H.-J. Steinhoff Structural insights into the early steps of receptor–transducer signal transfer in archaeal phototaxis EMBO J. 2001 20 5312-5319.
    • (2001) EMBO J. , vol.20 , pp. 5312-5319
    • Wegener, A.A.1    Klare, J.P.2    Engelhard, M.3    Steinhoff, H.-J.4
  • 18
    • 0035960642 scopus 로고    scopus 로고
    • Light-induced structural changes occur in the transmembrane helices of the Natronobacterium pharaonis HtrII transducer
    • C.-S. Yang J. L. Spudich Light-induced structural changes occur in the transmembrane helices of the Natronobacterium pharaonis HtrII transducer Biochemistry 2001 40 14207-14214.
    • (2001) Biochemistry , vol.40 , pp. 14207-14214
    • Yang, C.-S.1    Spudich, J.L.2
  • 19
    • 0035943457 scopus 로고    scopus 로고
    • Crystal structure of sensory rhodopsin II at 2.4 Å: Insights into color tuning and transducer interaction
    • H. Luecke B. Schobert J. K. Lanyi E. N. Spudich J. L. Spudich Crystal structure of sensory rhodopsin II at 2.4 Å: Insights into color tuning and transducer interaction Science 2001 293 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
  • 22
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • D. L. Farrens C. Altenbach K. Yang W. L. Hubbell H. G. Khorana Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin Science 1996 274 768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 23
    • 0037282379 scopus 로고    scopus 로고
    • Force and voltage sensors in one structure
    • F. Bezanilla E. Perozo Force and voltage sensors in one structure Adv. Protein Chem. 2003 63 211-241.
    • (2003) Adv. Protein Chem. , vol.63 , pp. 211-241
    • Bezanilla, F.1    Perozo, E.2
  • 24
    • 0035951101 scopus 로고    scopus 로고
    • Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: Experimental strategies and practical limitations
    • C. Altenbach J. Klein-Seetharaman K. W. Cai H. G. Khorana W. L. Hubbell Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: Experimental strategies and practical limitations Biochemistry 2001 40 15493-15500.
    • (2001) Biochemistry , vol.40 , pp. 15493-15500
    • Altenbach, C.1    Klein-Seetharaman, J.2    Cai, K.W.3    Khorana, H.G.4    Hubbell, W.L.5
  • 26
    • 0030781782 scopus 로고    scopus 로고
    • Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the X-ray structure
    • H.-J. Steinhoff N. Radzwill W. Thevis V. Lenz D. Brandenburg A. Antson G. Dodson A. Wollmer Determination of interspin distances between spin labels attached to insulin: comparison of electron paramagnetic resonance data with the X-ray structure Biophys. J. 1997 73 3287-3298.
    • (1997) Biophys. J. , vol.73 , pp. 3287-3298
    • Steinhoff, H.-J.1    Radzwill, N.2    Thevis, W.3    Lenz, V.4    Brandenburg, D.5    Antson, A.6    Dodson, G.7    Wollmer, A.8
  • 27
    • 0037177209 scopus 로고    scopus 로고
    • Demonstration of 2 : 2 stoichiometry in the functional SRI–HtrI signaling complex in Halobacterium membranes by gene fusion analysis
    • X. Chen J. L. Spudich Demonstration of 2 : 2 stoichiometry in the functional SRI–HtrI signaling complex in Halobacterium membranes by gene fusion analysis Biochemistry 2002 41 3891-3896.
    • (2002) Biochemistry , vol.41 , pp. 3891-3896
    • Chen, X.1    Spudich, J.L.2
  • 28
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers – crystal structure of the bacteriorhodopsin-lipid complex
    • L. O. Essen R. Siegert W. D. Lehmannn D. Oesterhelt Lipid patches in membrane protein oligomers – crystal structure of the bacteriorhodopsin-lipid complex Proc. Natl. Acad. Sci. USA 1998 95 11673-11678.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11673-11678
    • Essen, L.O.1    Siegert, R.2    Lehmannn, W.D.3    Oesterhelt, D.4
  • 29
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • E. M. Landau J. P. Rosenbusch Lipidic cubic phases: A novel concept for the crystallization of membrane proteins Proc. Natl. Acad. Sci. USA 1996 93 14532-14535.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 30
    • 0026331216 scopus 로고
    • Identification of signaling states of a sensory receptor by modulation of lifetimes of stimulus-induced conformations: The case of sensory rhodopsin II
    • B. Yan T. Takahashi R. Johnson J. L. Spudich Identification of signaling states of a sensory receptor by modulation of lifetimes of stimulus-induced conformations: The case of sensory rhodopsin II Biochemistry 1991 30 10686-10692.
    • (1991) Biochemistry , vol.30 , pp. 10686-10692
    • Yan, B.1    Takahashi, T.2    Johnson, R.3    Spudich, J.L.4
  • 32
    • 0031820941 scopus 로고    scopus 로고
    • The photophobic receptor from Natronobacterium pharaonis: Temperature and pH dependencies of the photocycle of sensory rhodopsin II
    • I. Chizhov G. Schmies R. Seidel J. R. Sydor B. Lüttenberg M. Engelhard The photophobic receptor from Natronobacterium pharaonis: Temperature and pH dependencies of the photocycle of sensory rhodopsin II Biophys. J. 1998 75 999-1009.
    • (1998) Biophys. J. , vol.75 , pp. 999-1009
    • Chizhov, I.1    Schmies, G.2    Seidel, R.3    Sydor, J.R.4    Lüttenberg, B.5    Engelhard, M.6
  • 35
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • S. Subramaniam R. Henderson Molecular mechanism of vectorial proton translocation by bacteriorhodopsin Nature 2000 406 653-657.
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 37
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution
    • H. Luecke B. Schobert H. T. Richter J. P. Cartailler J. K. Lanyi Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution Science 1999 286 255-261.
    • (1999) Science , vol.286 , pp. 255-261
    • Luecke, H.1    Schobert, B.2    Richter, H.T.3    Cartailler, J.P.4    Lanyi, J.K.5
  • 38
    • 0035016932 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin
    • N. Radzwill K. Gerwert H.-J. Steinhoff Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin Biophys. J. 2001 80 2856-2866.
    • (2001) Biophys. J. , vol.80 , pp. 2856-2866
    • Radzwill, N.1    Gerwert, K.2    Steinhoff, H.-J.3
  • 39
    • 0034009519 scopus 로고    scopus 로고
    • Unraveling photoexcited conformational changes of bacteriorhodopsin by time resolved electron paramagnetic resonance spectroscopy
    • T. Rink M. Pfeiffer D. Oesterhelt K. Gerwert H.-J. Steinhoff Unraveling photoexcited conformational changes of bacteriorhodopsin by time resolved electron paramagnetic resonance spectroscopy Biophys. J. 2000 78 1519-1530.
    • (2000) Biophys. J. , vol.78 , pp. 1519-1530
    • Rink, T.1    Pfeiffer, M.2    Oesterhelt, D.3    Gerwert, K.4    Steinhoff, H.-J.5
  • 40
    • 0029865503 scopus 로고    scopus 로고
    • Molecular mechanism of transmembrane signaling by the aspartate receptor: A model
    • S. A. Chervitz J. J. Falke Molecular mechanism of transmembrane signaling by the aspartate receptor: A model Proc. Natl. Acad. Sci. USA 1996 93 2545-2550.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2545-2550
    • Chervitz, S.A.1    Falke, J.J.2
  • 41
    • 0033543590 scopus 로고    scopus 로고
    • A piston model for transmembrane signaling of the aspartate receptor
    • K. M. Ottemann W. Xiao Y. K. Shin D. E. J. Koshland A piston model for transmembrane signaling of the aspartate receptor Science 1999 285 1751-1754.
    • (1999) Science , vol.285 , pp. 1751-1754
    • Ottemann, K.M.1    Xiao, W.2    Shin, Y.K.3    Koshland, D.E.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.