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Volumn 45, Issue 11, 2006, Pages 3542-3547

The crystal structure of the R52Q mutant demonstrates a role for R52 in chromophore pKa regulation in photoactive yellow protein

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; CHROMOPHORES; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; HYDROGEN BONDS; PH EFFECTS; PROTEINS;

EID: 33645214376     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051430a     Document Type: Article
Times cited : (23)

References (31)
  • 1
    • 0022430790 scopus 로고
    • Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila
    • Meyer, T. E. (1985) Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila, Biochim. Biophys. Acta 806, 175-183.
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 175-183
    • Meyer, T.E.1
  • 2
    • 0027324441 scopus 로고
    • The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein
    • Sprenger, W. W., Hoff, W. D., Armitage, J. P., and Hellingwerf, K. J. (1993) The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein, J. Bacteriol. 175, 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
  • 3
    • 0029110488 scopus 로고
    • 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
    • Borgstahl, G. E. O., Williams, D. R., and Getzoff, E. D. (1995) 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore, Biochemistry 34, 6278-6287.
    • (1995) Biochemistry , vol.34 , pp. 6278-6287
    • Borgstahl, G.E.O.1    Williams, D.R.2    Getzoff, E.D.3
  • 4
    • 0033974163 scopus 로고    scopus 로고
    • Conformational substrates in different crystal forms of the photoactive yellow protein-correlation with theoretical and experimental flexibility
    • Van Aalten, D., Crielaard, W., Hellingwerf, K. J., and Joshua-Tor, L. (2000) Conformational substrates in different crystal forms of the photoactive yellow protein-correlation with theoretical and experimental flexibility, Protein Sci. 9, 64-72.
    • (2000) Protein Sci. , vol.9 , pp. 64-72
    • Van Aalten, D.1    Crielaard, W.2    Hellingwerf, K.J.3    Joshua-Tor, L.4
  • 7
    • 0028577744 scopus 로고
    • Complete chemical structure of photoactive yellow protein: Novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry
    • Baca, M., Borgstahl, G. E. O., Boissinot, M., Burke, P. M., Williams, D. R., Slater, K. A., and Getzoff, E. D. (1994) Complete chemical structure of photoactive yellow protein: Novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry, Biochemistry 33, 14369-14377.
    • (1994) Biochemistry , vol.33 , pp. 14369-14377
    • Baca, M.1    Borgstahl, G.E.O.2    Boissinot, M.3    Burke, P.M.4    Williams, D.R.5    Slater, K.A.6    Getzoff, E.D.7
  • 8
    • 0028868422 scopus 로고
    • Reconstitution photoactive yellow protein from apoprotein and p-coumaric acid derivatives
    • Imamoto, Y., Ito, T., Kataoka, M., and Tokunaga, F. (1995) Reconstitution photoactive yellow protein from apoprotein and p-coumaric acid derivatives, FEBS Lett. 374, 157-160.
    • (1995) FEBS Lett. , vol.374 , pp. 157-160
    • Imamoto, Y.1    Ito, T.2    Kataoka, M.3    Tokunaga, F.4
  • 9
    • 0029731183 scopus 로고    scopus 로고
    • Spectral tuning, fluorescence, and photoactivity in hybrids of photoactive yellow protein, reconstituted with native or modified chromophores
    • Kroon, A. R., Hoff, W. D., Fennema, H. P., Gijzen, J., Koomen, G. J., Verhoeven, J. W., Crielaard, W., and Hellingwerf, K. J. (1996) Spectral tuning, fluorescence, and photoactivity in hybrids of photoactive yellow protein, reconstituted with native or modified chromophores, J. Biol. Chem. 271, 31949-31956.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31949-31956
    • Kroon, A.R.1    Hoff, W.D.2    Fennema, H.P.3    Gijzen, J.4    Koomen, G.J.5    Verhoeven, J.W.6    Crielaard, W.7    Hellingwerf, K.J.8
  • 11
    • 0029803844 scopus 로고    scopus 로고
    • Photoreaction cycle of photoactive yellow protein from Ectothiorhodospira halophila studied by low-temperature spectroscopy
    • Imamoto, Y., Kataoka, M., and Tokunaga, F. (1996) Photoreaction cycle of photoactive yellow protein from Ectothiorhodospira halophila studied by low-temperature spectroscopy, Biochemistry 35, 14047-14053.
    • (1996) Biochemistry , vol.35 , pp. 14047-14053
    • Imamoto, Y.1    Kataoka, M.2    Tokunaga, F.3
  • 12
    • 0031808072 scopus 로고    scopus 로고
    • New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: Picosecond transient absorption spectroscopy
    • Ujj, L., Devanathan, S., Meyer, T. E., Cusanovich, M. A., Tollin, G., and Atkinson, G. H. (1998) New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: Picosecond transient absorption spectroscopy, Biophys. J. 75, 406-412.
    • (1998) Biophys. J. , vol.75 , pp. 406-412
    • Ujj, L.1    Devanathan, S.2    Meyer, T.E.3    Cusanovich, M.A.4    Tollin, G.5    Atkinson, G.H.6
  • 13
    • 0035918547 scopus 로고    scopus 로고
    • Primary photoreaction of photoactive yellow protein studied by subpicosecond-nanosecond spectroscopy
    • Imamoto, Y., Kataoka, M., Tokunaga, F., Asahi, T., and Masuhara, H. (2001) Primary photoreaction of photoactive yellow protein studied by subpicosecond-nanosecond spectroscopy, Biochemistry 40, 6047-6052.
    • (2001) Biochemistry , vol.40 , pp. 6047-6052
    • Imamoto, Y.1    Kataoka, M.2    Tokunaga, F.3    Asahi, T.4    Masuhara, H.5
  • 14
    • 0035979371 scopus 로고    scopus 로고
    • Low-temperature Fourier transform infrared spectroscopy of photoactive yellow protein
    • Imamoto, Y., Shirahige, Y., Tokunaga, F., Kinoshita, T., Yoshihara, K., and Kataoka, M. (2001) Low-temperature Fourier transform infrared spectroscopy of photoactive yellow protein, Biochemistry 40, 8997-9004.
    • (2001) Biochemistry , vol.40 , pp. 8997-9004
    • Imamoto, Y.1    Shirahige, Y.2    Tokunaga, F.3    Kinoshita, T.4    Yoshihara, K.5    Kataoka, M.6
  • 15
    • 0030446427 scopus 로고    scopus 로고
    • Glu46 donates a proton to the 4-hydroxycinnamate anion chromophore during the photocycle of photoactive yellow protein
    • Xie, A., Hoff, W. D., Kroon, A. R., and Hellingwerf, K. J. (1996) Glu46 donates a proton to the 4-hydroxycinnamate anion chromophore during the photocycle of photoactive yellow protein, Biochemistry 35, 14671-14678.
    • (1996) Biochemistry , vol.35 , pp. 14671-14678
    • Xie, A.1    Hoff, W.D.2    Kroon, A.R.3    Hellingwerf, K.J.4
  • 16
    • 0031011485 scopus 로고    scopus 로고
    • Evidence for proton transfer from Glu-46 to the chromophore during the photocycle of photoactive yellow protein
    • Imamoto, Y., Mihara, K., Hisatomi, O., Kataoka, M., Tokunaga, F., Bojkova, N., and Yoshihara, K. (1997) Evidence for proton transfer from Glu-46 to the chromophore during the photocycle of photoactive yellow protein, J. Biol. Chem. 272, 12905-12908.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12905-12908
    • Imamoto, Y.1    Mihara, K.2    Hisatomi, O.3    Kataoka, M.4    Tokunaga, F.5    Bojkova, N.6    Yoshihara, K.7
  • 17
    • 0034745934 scopus 로고    scopus 로고
    • Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy
    • Brudler, R., Rammelsberg, R., Woo, T. T., Getzoff, E. D., and Gerwert, K. (2001) Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy, Nat. Struct. Biol. 8, 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
  • 18
    • 0035852878 scopus 로고    scopus 로고
    • Formation of a new buried charge drives a large-amplitude protein quake in photoreceptor activation
    • Xie, A., Kelemen, L., Hendriks, J., White, B. J., Hellingwerf, K. J., and Hoff, W. D. (2001) Formation of a new buried charge drives a large-amplitude protein quake in photoreceptor activation, Biochemistry 40, 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
  • 20
    • 0036685014 scopus 로고    scopus 로고
    • Effect of organic anions on the photoreaction of photoactive yellow protein
    • Shimizu, N., Kamikubo, H., Mihara, K., Imamoto, Y., and Kataoka, M. (2002) Effect of Organic Anions on the Photoreaction of Photoactive Yellow Protein, J. Biochem. 132, 257-263.
    • (2002) J. Biochem. , vol.132 , pp. 257-263
    • Shimizu, N.1    Kamikubo, H.2    Mihara, K.3    Imamoto, Y.4    Kataoka, M.5
  • 21
    • 0030914406 scopus 로고    scopus 로고
    • Functional expression and site-directed mutagenesis of photoactive yellow protein
    • Mihara, K., Hisatomi, O., Imamoto, Y., Kataoka, M., and Tokunaga, F. (1997) Functional expression and site-directed mutagenesis of photoactive yellow protein, J. Biochem. 121, 876-880.
    • (1997) J. Biochem. , vol.121 , pp. 876-880
    • Mihara, K.1    Hisatomi, O.2    Imamoto, Y.3    Kataoka, M.4    Tokunaga, F.5
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: An automated package for molecular replacement, Acta Crystallogr. A50, 157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 26
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallogr. D53, 240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 27
    • 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., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 29
    • 0029185933 scopus 로고
    • CRYSOL: A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., Barberato, C., and Koch, M. H. J. (1995) CRYSOL: A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates, J. Appl. Crystallogr. 28, 768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 31
    • 2942599831 scopus 로고    scopus 로고
    • Short hydrogen bonds in photoactive yellow protein
    • Anderson, S., Crosson, S., and Moffat, K. (2004) Short hydrogen bonds in photoactive yellow protein, Acta Crystallogr. D60, 1008-1016.
    • (2004) Acta Crystallogr. , vol.D60 , pp. 1008-1016
    • Anderson, S.1    Crosson, S.2    Moffat, K.3


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