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Volumn 463, Issue 7278, 2010, Pages 250-254

Structural basis for the photoconversion of a phytochrome to the activated Pfr form

Author keywords

[No Author keywords available]

Indexed keywords

PHYTOCHROME; PYRROLE;

EID: 74549198962     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08671     Document Type: Article
Times cited : (119)

References (45)
  • 3
    • 55749108535 scopus 로고    scopus 로고
    • The structure of a complete phytochrome sensory module in the Pr ground state
    • Essen, L. O., Mailliet, J. & Hughes, J. The structure of a complete phytochrome sensory module in the Pr ground state. Proc. Natl Acad. Sci. USA 105, 14709-14714 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 14709-14714
    • Essen, L.O.1    Mailliet, J.2    Hughes, J.3
  • 4
    • 52949096101 scopus 로고    scopus 로고
    • Solution structure of a cyanobacterial phytochrome GAF domain in the red-light-absorbing ground state
    • Cornilescu, G., Ulijasz, A. T., Cornilescu, C. C., Markley, J. L. & Vierstra, R. D. Solution structure of a cyanobacterial phytochrome GAF domain in the red-light-absorbing ground state. J. Mol. Biol. 383, 403-413 (2008).
    • (2008) J. Mol. Biol. , vol.383 , pp. 403-413
    • Cornilescu, G.1    Ulijasz, A.T.2    Cornilescu, C.C.3    Markley, J.L.4    Vierstra, R.D.5
  • 5
    • 27844461604 scopus 로고    scopus 로고
    • A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome
    • Wagner, J. R., Brunzelle, J. S., Forest, K. T. & Vierstra, R. D. A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome. Nature 438, 325-331 (2005).
    • (2005) Nature , vol.438 , pp. 325-331
    • Wagner, J.R.1    Brunzelle, J.S.2    Forest, K.T.3    Vierstra, R.D.4
  • 6
    • 34249728355 scopus 로고    scopus 로고
    • High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution
    • Wagner, J. R., Zhang, J., Brunzelle, J. S., Vierstra, R. D. & Forest, K. T. High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution. J. Biol. Chem. 282, 12298-12309 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 12298-12309
    • Wagner, J.R.1    Zhang, J.2    Brunzelle, J.S.3    Vierstra, R.D.4    Forest, K.T.5
  • 7
    • 55749108880 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: Photoconversion and signal transduction
    • Yang, X., Kuk, J. & Moffat, K. Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction. Proc. Natl Acad. Sci. USA 105, 14715-14720 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 14715-14720
    • Yang, X.1    Kuk, J.2    Moffat, K.3
  • 8
    • 0036484368 scopus 로고    scopus 로고
    • Phytochrome photosensory signalling networks
    • Quail, P. H. Phytochrome photosensory signalling networks. Nature Rev. Mol. Cell Biol. 3, 85-93 (2002).
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 85-93
    • Quail, P.H.1
  • 10
    • 0033576250 scopus 로고    scopus 로고
    • Protonation state and structural changes of the tetrapyrrole chromophore during the Pr R Pfr phototransformation of phytochrome: A resonance Raman spectroscopic study
    • Kneip, C. et al. Protonation state and structural changes of the tetrapyrrole chromophore during the Pr R Pfr phototransformation of phytochrome: a resonance Raman spectroscopic study. Biochemistry 38, 15185-15192 (1999).
    • (1999) Biochemistry , vol.38 , pp. 15185-15192
    • Kneip, C.1
  • 11
    • 21644470824 scopus 로고    scopus 로고
    • Sterically locked synthetic bilin derivatives and phytochrome Agp1 from Agrobacterium tumefaciens form photosensitive Pr-and Pfr-like adducts
    • Inomata, K. et al. Sterically locked synthetic bilin derivatives and phytochrome Agp1 from Agrobacterium tumefaciens form photosensitive Pr-and Pfr-like adducts. J. Biol. Chem. 280, 24491-24497 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 24491-24497
    • Inomata, K.1
  • 12
    • 33748767100 scopus 로고    scopus 로고
    • Assembly of synthetic locked chromophores with Agrobacterium phytochromes Agp1 and Agp2
    • Inomata, K. et al. Assembly of synthetic locked chromophores with Agrobacterium phytochromes Agp1 and Agp2. J. Biol. Chem. 281, 28162-28173 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 28162-28173
    • Inomata, K.1
  • 13
    • 0025606743 scopus 로고
    • Resonance Raman analysis of the Pr and Pfr forms of phytochrome
    • Fodor, S. P., Lagarias, J. C. & Mathies, R. A. Resonance Raman analysis of the Pr and Pfr forms of phytochrome. Biochemistry 29, 11141-11146 (1990).
    • (1990) Biochemistry , vol.29 , pp. 11141-11146
    • Fodor, S.P.1    Lagarias, J.C.2    Mathies, R.A.3
  • 14
    • 70349461175 scopus 로고    scopus 로고
    • Conformational differences between the Pfr and Pr states of Pseudomonas aeruginosa bacteriophytochrome
    • Yang, X., Kuk, J. & Moffat, K. Conformational differences between the Pfr and Pr states of Pseudomonas aeruginosa bacteriophytochrome. Proc. Natl Acad. Sci. USA 106, 15639-15644 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 15639-15644
    • Yang, X.1    Kuk, J.2    Moffat, K.3
  • 15
    • 51049115356 scopus 로고    scopus 로고
    • Characterization of two thermostable cyanobacterial phytochromes reveals global movements in the chromophore-binding domain during photoconversion
    • Ulijasz, A. T. et al. Characterization of two thermostable cyanobacterial phytochromes reveals global movements in the chromophore-binding domain during photoconversion. J. Biol. Chem. 283, 21251-21266 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 21251-21266
    • Ulijasz, A.T.1
  • 16
    • 45549107695 scopus 로고    scopus 로고
    • Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for the photochromicity and proton exchange cycle of phytochromes
    • Wagner, J. R. et al. Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for the photochromicity and proton exchange cycle of phytochromes. J. Biol. Chem. 283, 12212-12226 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 12212-12226
    • Wagner, J.R.1
  • 17
    • 33847332642 scopus 로고    scopus 로고
    • Highly conserved residues Asp-197 and His-250 in Agp1 phytochrome control the proton affinity of the chromophore and Pfr formation
    • von Stetten, D. et al. Highly conserved residues Asp-197 and His-250 in Agp1 phytochrome control the proton affinity of the chromophore and Pfr formation. J. Biol. Chem. 282, 2116-2123 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 2116-2123
    • Von Stetten, D.1
  • 18
    • 0035949646 scopus 로고    scopus 로고
    • Light-induced proton release and proton uptake reactions in the cyanobacterial phytochrome Cph1
    • van Thor, J. J. et al. Light-induced proton release and proton uptake reactions in the cyanobacterial phytochrome Cph1. Biochemistry 40, 11460-11471 (2001).
    • (2001) Biochemistry , vol.40 , pp. 11460-11471
    • Van Thor, J.J.1
  • 19
    • 26644459239 scopus 로고    scopus 로고
    • Light-induced proton release of phytochrome is coupled to the transient deprotonation of the tetrapyrrole chromophore
    • Borucki, B. et al. Light-induced proton release of phytochrome is coupled to the transient deprotonation of the tetrapyrrole chromophore. J. Biol. Chem. 280, 34358-34364 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 34358-34364
    • Borucki, B.1
  • 20
    • 27944447344 scopus 로고    scopus 로고
    • Multiple roles of a conserved GAF domain tyrosine residue in cyanobacterial and plant phytochromes
    • Fischer, A. J. et al. Multiple roles of a conserved GAF domain tyrosine residue in cyanobacterial and plant phytochromes. Biochemistry 44, 15203-15215 (2005).
    • (2005) Biochemistry , vol.44 , pp. 15203-15215
    • Fischer, A.J.1
  • 21
    • 50849131895 scopus 로고    scopus 로고
    • Mutant screen distinguishes between residues necessary for light-signal perception and signal transfer by phytochrome B
    • Oka, Y., Matsushita, T., Mochizuki, N., Quail, P. H. & Nagatani, A. Mutant screen distinguishes between residues necessary for light-signal perception and signal transfer by phytochrome B. PLoS Genet. 4, e1000158 (2008).
    • (2008) PLoS Genet. , vol.4
    • Oka, Y.1    Matsushita, T.2    Mochizuki, N.3    Quail, P.H.4    Nagatani, A.5
  • 22
    • 27144507187 scopus 로고    scopus 로고
    • Phylogenetic analysis of the phytochrome superfamily reveals distinct microbial subfamilies of photoreceptors
    • Karniol, B., Wagner, J. R., Walker, J. M. & Vierstra, R. D. Phylogenetic analysis of the phytochrome superfamily reveals distinct microbial subfamilies of photoreceptors. Biochem. J. 392, 103-116 (2005).
    • (2005) Biochem. J. , vol.392 , pp. 103-116
    • Karniol, B.1    Wagner, J.R.2    Walker, J.M.3    Vierstra, R.D.4
  • 23
    • 55749110269 scopus 로고    scopus 로고
    • 15N magic-angle spinning NMR
    • 15N magic-angle spinning NMR. Proc. Natl Acad. Sci. USA 105, 15229-15234 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 15229-15234
    • Rohmer, T.1
  • 24
    • 36049048341 scopus 로고    scopus 로고
    • C transition in the functional cycle of bacteriophytochrome Agp1
    • C transition in the functional cycle of bacteriophytochrome Agp1. FEBS Lett. 581, 5425-5429 (2007).
    • (2007) FEBS Lett. , vol.581 , pp. 5425-5429
    • Seibeck, S.1
  • 25
    • 65249186449 scopus 로고    scopus 로고
    • Assembly of Agrobacterium phytochromes Agp1 and Agp2 with doubly locked bilin chromophores
    • Inomata, K. et al. Assembly of Agrobacterium phytochromes Agp1 and Agp2 with doubly locked bilin chromophores. Biochemistry 48, 2817-2827 (2009).
    • (2009) Biochemistry , vol.48 , pp. 2817-2827
    • Inomata, K.1
  • 26
    • 33748450550 scopus 로고    scopus 로고
    • Chromophore structure in the photocycle of the cyanobacterial phytochrome Cph1
    • van Thor, J. J., Mackeen, M., Kuprov, I., Dwek, R. A. & Wormald, M. R. Chromophore structure in the photocycle of the cyanobacterial phytochrome Cph1. Biophys. J. 91, 1811-1822 (2006).
    • (2006) Biophys. J. , vol.91 , pp. 1811-1822
    • Van Thor, J.J.1    MacKeen, M.2    Kuprov, I.3    Dwek, R.A.4    Wormald, M.R.5
  • 27
    • 20444369555 scopus 로고    scopus 로고
    • Heteronuclear solution-state NMR studies of the chromophore in cyanobacterial phytochrome Cph1
    • Strauss, H. M., Hughes, J. & Schmieder, P. Heteronuclear solution-state NMR studies of the chromophore in cyanobacterial phytochrome Cph1. Biochemistry 44, 8244-8250 (2005).
    • (2005) Biochemistry , vol.44 , pp. 8244-8250
    • Strauss, H.M.1    Hughes, J.2    Schmieder, P.3
  • 28
    • 34547628072 scopus 로고    scopus 로고
    • Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion
    • Yang, X., Stojkovic, E. A., Kuk, J. & Moffat, K. Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion. Proc. Natl Acad. Sci. USA 104, 12571-12576 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 12571-12576
    • Yang, X.1    Stojkovic, E.A.2    Kuk, J.3    Moffat, K.4
  • 29
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper, S. M., Neil, L. C. & Gardner, K. H. Structural basis of a phototropin light switch. Science 301, 1541-1544 (2003).
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 30
    • 17844374336 scopus 로고    scopus 로고
    • Predicting the signaling state of photoactive yellow protein
    • Vreede, J., Crielaard, W., Hellingwerf, K. J. & Bolhuis, P. G. Predicting the signaling state of photoactive yellow protein. Biophys. J. 88, 3525-3535 (2005).
    • (2005) Biophys. J. , vol.88 , pp. 3525-3535
    • Vreede, J.1    Crielaard, W.2    Hellingwerf, K.J.3    Bolhuis, P.G.4
  • 31
    • 52949096101 scopus 로고    scopus 로고
    • Solution structure of a cyanobacterial phytochrome GAF domain in the red-light-absorbing ground state
    • Cornilescu, G., Ulijasz, A. T., Cornilescu, C. C., Markley, J. L. & Vierstra, R. D. Solution structure of a cyanobacterial phytochrome GAF domain in the red-light-absorbing ground state. J. Mol. Biol. 383, 403-413 (2008).
    • (2008) J. Mol. Biol. , vol.383 , pp. 403-413
    • Cornilescu, G.1    Ulijasz, A.T.2    Cornilescu, C.C.3    Markley, J.L.4    Vierstra, R.D.5
  • 32
    • 51049115356 scopus 로고    scopus 로고
    • Characterization of two thermostable cyanobacterial phytochromes reveals global movements in the chromophore-binding domain during photoconversion
    • Ulijasz, A. T. et al. Characterization of two thermostable cyanobacterial phytochromes reveals global movements in the chromophore-binding domain during photoconversion. J. Biol. Chem. 283, 21251-21266 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 21251-21266
    • Ulijasz, A.T.1
  • 33
    • 0042367594 scopus 로고    scopus 로고
    • Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy
    • Ulmer, T. S., Ramirez, B. E., Delaglio, F. & Bax, A. Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy. J. Am. Chem. Soc. 125, 9179-9191 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9179-9191
    • Ulmer, T.S.1    Ramirez, B.E.2    Delaglio, F.3    Bax, A.4
  • 34
    • 0034684181 scopus 로고    scopus 로고
    • Measurement of proton, nitrogen, and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase
    • Cornilescu, G. & Bax, A. Measurement of proton, nitrogen, and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase. J. Am. Chem. Soc. 122, 10143-10154 (2000).
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 10143-10154
    • Cornilescu, G.1    Bax, A.2
  • 35
    • 0032185144 scopus 로고    scopus 로고
    • Measurement of dipolar couplings for methylene and methyl sites in weakly oriented macromolecules and their use in structure determination
    • Ottiger, M., Delaglio, F., Marquardt, J. L., Tjandra, N. & Bax, A. Measurement of dipolar couplings for methylene and methyl sites in weakly oriented macromolecules and their use in structure determination. J. Magn. Reson. 134, 365-369 (1998).
    • (1998) J. Magn. Reson. , vol.134 , pp. 365-369
    • Ottiger, M.1    Delaglio, F.2    Marquardt, J.L.3    Tjandra, N.4    Bax, A.5
  • 36
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F. & Bax, A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302 (1999).
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 38
    • 0022826066 scopus 로고
    • Phycobiliprotein-bilin linkage diversity. I. Structural studies on A-and D-ring-linked phycocyanobilins
    • Bishop, J. E. et al. Phycobiliprotein-bilin linkage diversity. I. Structural studies on A-and D-ring-linked phycocyanobilins. J. Biol. Chem. 261, 6790-6796 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 6790-6796
    • Bishop, J.E.1
  • 39
    • 0003105697 scopus 로고
    • Chromopeptides from C-phycocyanin. Structure and linkage of a phycocyanobilin bound to the b subunit
    • Lagarias, J. C., Glazer, A. N. & Rapoport, H. Chromopeptides from C-phycocyanin. Structure and linkage of a phycocyanobilin bound to the b subunit. J. Am. Chem. Soc. 101, 5030-5037 (1979).
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 5030-5037
    • Lagarias, J.C.1    Glazer, A.N.2    Rapoport, H.3
  • 41
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf, A. W. & van Aalten, D. M. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D 60, 1355-1363 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 42
    • 0000041361 scopus 로고
    • A common sense approach to peak picking two-, three-and four-dimensional spectra using automatic computer analysis of contour diagrams
    • Garrett, D. S., Powers, R., Gronenborn, A. M. & Clore, G. M. A common sense approach to peak picking two-, three-and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95, 214-220 (1991).
    • (1991) J. Magn. Reson. , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 43
    • 0033026167 scopus 로고    scopus 로고
    • Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values
    • Ottiger, M. & Bax, A. Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values. J. Biomol. NMR 13, 187-191 (1999).
    • (1999) J. Biomol. NMR , vol.13 , pp. 187-191
    • Ottiger, M.1    Bax, A.2
  • 44
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra, N. & Bax, A. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278, 1111-1114 (1997).
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 45
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291 (1993).
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


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