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Volumn 13, Issue 1, 2005, Pages 55-63

A structural pathway for signaling in the E46Q mutant of photoactive yellow protein

Author keywords

[No Author keywords available]

Indexed keywords

PHOTOACTIVE YELLOW PROTEIN;

EID: 11844294715     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2004.10.016     Document Type: Article
Times cited : (66)

References (45)
  • 1
  • 3
    • 2942533032 scopus 로고    scopus 로고
    • Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein
    • S. Anderson, V. Srajer, R. Pahl, S. Rajagopal, F. Schotte, P. Anfinrud, M. Wulff, and K. Moffat Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein Structure 12 2004 1039 1045
    • (2004) Structure , vol.12 , pp. 1039-1045
    • Anderson, S.1    Srajer, V.2    Pahl, R.3    Rajagopal, S.4    Schotte, F.5    Anfinrud, P.6    Wulff, M.7    Moffat, K.8
  • 4
    • 0035345448 scopus 로고    scopus 로고
    • Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures
    • S.P. Balashov, and T.G. Ebrey Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures Photochem. Photobiol. 73 2001 453 462
    • (2001) Photochem. Photobiol. , vol.73 , pp. 453-462
    • Balashov, S.P.1    Ebrey, T.G.2
  • 5
    • 0034745934 scopus 로고    scopus 로고
    • Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy
    • R. Brudler, R. Rammelsberg, T.T. Woo, E.D. Getzoff, and K. Gerwert Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy Nat. Struct. Biol. 8 2001 265 270
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 265-270
    • Brudler, R.1    Rammelsberg, R.2    Woo, T.T.3    Getzoff, E.D.4    Gerwert, K.5
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 7
    • 0028430176 scopus 로고
    • Optical monitoring of protein crystals in time-resolved x-ray experiments - Microspectrophotometer design and performance
    • Y. Chen, V. Srajer, K. Ng, A. Legrand, and K. Moffat Optical monitoring of protein crystals in time-resolved x-ray experiments - microspectrophotometer design and performance Rev. Sci. Instrum. 65 1994 1506 1511
    • (1994) Rev. Sci. Instrum. , vol.65 , pp. 1506-1511
    • Chen, Y.1    Srajer, V.2    Ng, K.3    Legrand, A.4    Moffat, K.5
  • 8
    • 0034727659 scopus 로고    scopus 로고
    • Probing the nature of the blue-shifted intermediate of photoactive yellow protein in solution by NMR: Hydrogen-deuterium exchange data and pH studies
    • C.J. Craven, N.M. Derix, J. Hendriks, R. Boelens, K.J. Hellingwerf, and R. Kaptein Probing the nature of the blue-shifted intermediate of photoactive yellow protein in solution by NMR: hydrogen-deuterium exchange data and pH studies Biochemistry 39 2000 14392 14399
    • (2000) Biochemistry , vol.39 , pp. 14392-14399
    • Craven, C.J.1    Derix, N.M.2    Hendriks, J.3    Boelens, R.4    Hellingwerf, K.J.5    Kaptein, R.6
  • 9
    • 0037435618 scopus 로고    scopus 로고
    • The LOV domain family: Photoresponsive signaling modules coupled to diverse output domains
    • S. Crosson, S. Rajagopal, and K. Moffat The LOV domain family: photoresponsive signaling modules coupled to diverse output domains Biochemistry 42 2003 2 10
    • (2003) Biochemistry , vol.42 , pp. 2-10
    • Crosson, S.1    Rajagopal, S.2    Moffat, K.3
  • 10
    • 0037657894 scopus 로고    scopus 로고
    • Photoactive yellow protein: A prototypic PAS domain sensory protein and development of a common signaling mechanism
    • M.A. Cusanovich, and T.E. Meyer Photoactive yellow protein: a prototypic PAS domain sensory protein and development of a common signaling mechanism Biochemistry 42 2003 4759 4770
    • (2003) Biochemistry , vol.42 , pp. 4759-4770
    • Cusanovich, M.A.1    Meyer, T.E.2
  • 11
    • 0346850583 scopus 로고    scopus 로고
    • Lack of negative charge in the E46Q mutant of photoactive yellow protein prevents partial unfolding of the blue-shifted intermediate
    • N.M. Derix, R.W. Wechselberger, M.A. van der Horst, K.J. Hellingwerf, R. Boelens, R. Kaptein, and N.A. van Nuland Lack of negative charge in the E46Q mutant of photoactive yellow protein prevents partial unfolding of the blue-shifted intermediate Biochemistry 42 2003 14501 14506
    • (2003) Biochemistry , vol.42 , pp. 14501-14506
    • Derix, N.M.1    Wechselberger, R.W.2    Van Der Horst, M.A.3    Hellingwerf, K.J.4    Boelens, R.5    Kaptein, R.6    Van Nuland, N.A.7
  • 12
    • 0035957014 scopus 로고    scopus 로고
    • The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin
    • H. Frauenfelder, B.H. McMahon, R.H. Austin, K. Chu, and J.T. Groves The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin Proc. Natl. Acad. Sci. USA 98 2001 2370 2374
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2370-2374
    • Frauenfelder, H.1    McMahon, B.H.2    Austin, R.H.3    Chu, K.4    Groves, J.T.5
  • 15
    • 0032510475 scopus 로고    scopus 로고
    • Structure at 0.85 Å resolution of an early protein photocycle intermediate
    • U.K. Genick, S.M. Soltis, P. Kuhn, I.L. Canestrelli, and E.D. Getzoff Structure at 0.85 Å resolution of an early protein photocycle intermediate Nature 392 1998 206 209
    • (1998) Nature , vol.392 , pp. 206-209
    • Genick, U.K.1    Soltis, S.M.2    Kuhn, P.3    Canestrelli, I.L.4    Getzoff, E.D.5
  • 17
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • S.M. Harper, L.C. Neil, and K.H. Gardner Structural basis of a phototropin light switch Science 301 2003 1541 1544
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 18
    • 0036427580 scopus 로고    scopus 로고
    • The molecular basis of sensing and responding to light in microorganisms
    • K.J. Hellingwerf The molecular basis of sensing and responding to light in microorganisms Antonie Van Leeuwenhoek 81 2002 51 59
    • (2002) Antonie Van Leeuwenhoek , vol.81 , pp. 51-59
    • Hellingwerf, K.J.1
  • 19
    • 0029743968 scopus 로고    scopus 로고
    • Photobiology of microorganisms: How photosensors catch a photon to initialize signalling
    • K.J. Hellingwerf, W.D. Hoff, and W. Crielaard Photobiology of microorganisms: how photosensors catch a photon to initialize signalling Mol. Microbiol. 21 1996 683 693
    • (1996) Mol. Microbiol. , vol.21 , pp. 683-693
    • Hellingwerf, K.J.1    Hoff, W.D.2    Crielaard, W.3
  • 20
    • 0037468225 scopus 로고    scopus 로고
    • Photoactive yellow protein, a new type of photoreceptor protein: Will this "yellow lab" bring us where we want to go?
    • K.J. Hellingwerf, J. Hendriks, and T. Gensch Photoactive yellow protein, a new type of photoreceptor protein: will this "yellow lab" bring us where we want to go? J. Phys. Chem. A 107 2003 1082 1094
    • (2003) J. Phys. Chem. a , vol.107 , pp. 1082-1094
    • Hellingwerf, K.J.1    Hendriks, J.2    Gensch, T.3
  • 21
    • 0026633609 scopus 로고
    • Singular value decomposition: Application to analysis of experimental data
    • E. Henry, and J. Hofrichter Singular value decomposition: application to analysis of experimental data Methods Enzymol. 210 1992 129 192
    • (1992) Methods Enzymol. , vol.210 , pp. 129-192
    • Henry, E.1    Hofrichter, J.2
  • 24
    • 0037137227 scopus 로고    scopus 로고
    • Light-induced global conformational change of photoactive yellow protein in solution
    • Y. Imamoto, H. Kamikubo, M. Harigai, N. Shimizu, and M. Kataoka Light-induced global conformational change of photoactive yellow protein in solution Biochemistry 41 2002 13595 13601
    • (2002) Biochemistry , vol.41 , pp. 13595-13601
    • Imamoto, Y.1    Kamikubo, H.2    Harigai, M.3    Shimizu, N.4    Kataoka, M.5
  • 25
    • 0036468436 scopus 로고    scopus 로고
    • The modular logic of signaling proteins: Building allosteric switches from simple binding domains
    • W.A. Lim The modular logic of signaling proteins: building allosteric switches from simple binding domains Curr. Opin. Struct. Biol. 12 2002 61 68
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 61-68
    • Lim, W.A.1
  • 26
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density
    • D.E. McRee XtalView/Xfit: a versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125 1999 156 165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 27
    • 0023152468 scopus 로고
    • Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin
    • T.E. Meyer, E. Yakali, M.A. Cusanovich, and G. Tollin Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin Biochemistry 26 1987 418 423
    • (1987) Biochemistry , vol.26 , pp. 418-423
    • Meyer, T.E.1    Yakali, E.2    Cusanovich, M.A.3    Tollin, G.4
  • 28
    • 4344645546 scopus 로고    scopus 로고
    • Analysis of experimental time-resolved crystallographic data by singular value decomposition
    • S. Rajagopal, M. Schmidt, S. Anderson, and K. Moffat Analysis of experimental time-resolved crystallographic data by singular value decomposition Acta Crystallogr. D Biol. Crystallogr. 60 2004 860 871
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 860-871
    • Rajagopal, S.1    Schmidt, M.2    Anderson, S.3    Moffat, K.4
  • 29
    • 4344653824 scopus 로고    scopus 로고
    • Analytical trapping: Extraction of time-independent structures from time-dependent crystallographic data
    • S. Rajagopal, K. Kostov, and K. Moffat Analytical trapping: extraction of time-independent structures from time-dependent crystallographic data J. Struct. Biol. 147 2004 211 222
    • (2004) J. Struct. Biol. , vol.147 , pp. 211-222
    • Rajagopal, S.1    Kostov, K.2    Moffat, K.3
  • 31
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of alpha helices
    • J.S. Richardson, and D.C. Richardson Amino acid preferences for specific locations at the ends of alpha helices Science 240 1988 1648 1652
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 33
    • 0034519834 scopus 로고    scopus 로고
    • Trapping intermediates in the crystal: Ligand binding to myoglobin
    • I. Schlichting, and K. Chu Trapping intermediates in the crystal: ligand binding to myoglobin Curr. Opin. Struct. Biol. 10 2000 744 752
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 744-752
    • Schlichting, I.1    Chu, K.2
  • 35
    • 0037342350 scopus 로고    scopus 로고
    • Application of singular value decomposition to the analysis of time- resolved macromolecular x-ray data
    • M. Schmidt, S. Rajagopal, Z. Ren, and K. Moffat Application of singular value decomposition to the analysis of time- resolved macromolecular x-ray data Biophys. J. 84 2003 2112 2129
    • (2003) Biophys. J. , vol.84 , pp. 2112-2129
    • Schmidt, M.1    Rajagopal, S.2    Ren, Z.3    Moffat, K.4
  • 38
    • 0027324441 scopus 로고
    • The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein
    • W.W. Sprenger, W.D. Hoff, J.P. Armitage, and K.J. Hellingwerf The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein J. Bacteriol. 175 1993 3096 3104
    • (1993) J. Bacteriol. , vol.175 , pp. 3096-3104
    • Sprenger, W.W.1    Hoff, W.D.2    Armitage, J.P.3    Hellingwerf, K.J.4
  • 39
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • B.L. Taylor, and I.B. Zhulin PAS domains: internal sensors of oxygen, redox potential, and light Microbiol. Mol. Biol. Rev. 63 1999 479 506
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 40
    • 0028801485 scopus 로고
    • Difference refinement- obtaining differences between 2 related structures
    • T.C. Terwilliger, and J. Berendzen Difference refinement- obtaining differences between 2 related structures Acta Crystallogr. D Biol. Crystallogr. 51 1995 609 618
    • (1995) Acta Crystallogr. D Biol. Crystallogr. , vol.51 , pp. 609-618
    • Terwilliger, T.C.1    Berendzen, J.2
  • 41
    • 2642571008 scopus 로고    scopus 로고
    • Resonance Raman evidence for two conformations involved in the L intermediate of photoactive yellow protein
    • M. Unno, M. Kumauchi, N. Hamada, F. Tokunaga, and S. Yamauchi Resonance Raman evidence for two conformations involved in the L intermediate of photoactive yellow protein J. Biol. Chem. 279 2004 23855 23858
    • (2004) J. Biol. Chem. , vol.279 , pp. 23855-23858
    • Unno, M.1    Kumauchi, M.2    Hamada, N.3    Tokunaga, F.4    Yamauchi, S.5
  • 42
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • A.A. Vaguine, J. Richelle, and S.J. Wodak SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model Acta Crystallogr. D Biol. Crystallogr. 55 1999 191 205
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 43
    • 0035906913 scopus 로고    scopus 로고
    • The role of the N-terminal domain of photoactive yellow protein in the transient partial unfolding during signalling state formation
    • M.A. van der Horst, I.H. van Stokkum, W. Crielaard, and K.J. Helling werf The role of the N-terminal domain of photoactive yellow protein in the transient partial unfolding during signalling state formation FEBS Lett. 497 2001 26 30
    • (2001) FEBS Lett. , vol.497 , pp. 26-30
    • Van Der Horst, M.A.1    Van Stokkum, I.H.2    Crielaard, W.3    Helling Werf, K.J.4
  • 45
    • 0035852878 scopus 로고    scopus 로고
    • Formation of a new buried charge drives a large-amplitude protein quake in photoreceptor activation
    • A. Xie, L. Kelemen, J. Hendriks, B.J. White, K.J. Hellingwerf, and W.D. Hoff Formation of a new buried charge drives a large-amplitude protein quake in photoreceptor activation Biochemistry 40 2001 1510 1517
    • (2001) Biochemistry , vol.40 , pp. 1510-1517
    • Xie, A.1    Kelemen, L.2    Hendriks, J.3    White, B.J.4    Hellingwerf, K.J.5    Hoff, W.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.