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Volumn 106, Issue 37, 2009, Pages 15639-15644

Conformational differences between the Pfr and Pr states in Pseudomonas aeruginosa bacteriophytochrome

Author keywords

Biliverdin; Photoconversion; Red light photoreceptor

Indexed keywords

BACTERIOPHYTOCHROME; BILIVERDIN; PHYTOCHROME; SERINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 70349461175     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0902178106     Document Type: Article
Times cited : (127)

References (30)
  • 1
    • 0036676141 scopus 로고    scopus 로고
    • Phytochrome ancestry: Sensors of bilins and light
    • Montgomery BL, Lagarias JC (2002) Phytochrome ancestry: Sensors of bilins and light. Trends Plant Sci 7:357-366.
    • (2002) Trends Plant Sci , vol.7 , pp. 357-366
    • Montgomery, B.L.1    Lagarias, J.C.2
  • 2
    • 0033397947 scopus 로고    scopus 로고
    • Prokaryotes and phytochrome. the connection to chromophores and signaling
    • Hughes J, Lamparter T (1999) Prokaryotes and phytochrome. The connection to chromophores and signaling. Plant Physiol 121:1059-1068. (Pubitemid 30018493)
    • (1999) Plant Physiology , vol.121 , Issue.4 , pp. 1059-1068
    • Hughes, J.1    Lamparter, T.2
  • 3
    • 0033601199 scopus 로고    scopus 로고
    • Bacteriophytochromes: Phytochrome-like photoreceptors from nonphotosynthetic eubacteria
    • DOI 10.1126/science.286.5449.2517
    • Davis SJ, Vener AV, Vierstra RD (1999) Bacteriophytochromes: Phytochrome-like photoreceptors from nonphotosynthetic eubacteria. Science 286:2517-2520. (Pubitemid 30026342)
    • (1999) Science , vol.286 , Issue.5449 , pp. 2517-2520
    • Davis, S.J.1    Vener, A.V.2    Vierstra, R.D.3
  • 4
    • 0035856979 scopus 로고    scopus 로고
    • Bacteriophytochromes are photochromic histidine kinases using a biliverdin chromophore
    • DOI 10.1038/414776a
    • Bhoo SH, Davis SJ, Walker J, Karniol B, Vierstra RD (2001) Bacteriophytochromes are photochromic histidine kinases using a biliverdin chromophore. Nature 414:776-779. (Pubitemid 34000778)
    • (2001) Nature , vol.414 , Issue.6865 , pp. 776-779
    • Bhoo, S.-H.1    Davis, S.J.2    Walker, J.3    Karniol, B.4    Vierstra, R.D.5
  • 6
    • 33645747157 scopus 로고    scopus 로고
    • The structure of phytochrome: A picture is worth a thousand spectra
    • DOI 10.1105/tpc.105.038513
    • Rockwell NC, Lagarias JC (2006) The structure of phytochrome: A picture is worth a thousand spectra. Plant Cell 18:4-14. (Pubitemid 43951311)
    • (2006) Plant Cell , vol.18 , Issue.1 , pp. 4-14
    • Rockwell, N.C.1    Lagarias, J.C.2
  • 7
    • 34047204715 scopus 로고    scopus 로고
    • Protein conformational changes of Agrobacterium phytochrome Agp1 during chromophore assembly and photoconversion
    • DOI 10.1021/bi602419x
    • Noack S, Michael N, Rosen R, Lamparter T (2007) Protein conformational changes of Agrobacterium phytochrome Agp1 during chromophore assembly and photoconversion. Biochemistry 46:4164-4176. (Pubitemid 46536078)
    • (2007) Biochemistry , vol.46 , Issue.13 , pp. 4164-4176
    • Noack, S.1    Michael, N.2    Rosen, R.3    Lamparter, T.4
  • 8
    • 34248359515 scopus 로고    scopus 로고
    • The chromophore structural changes during the photocycle of phytochrome: A combined resonance Raman and quantum chemical approach
    • Mroginski MA, Murgida DH, Hildebrandt P (2007) The chromophore structural changes during the photocycle of phytochrome: A combined resonance Raman and quantum chemical approach. Acc Chem Res 40:258-266.
    • (2007) Acc Chem Res , vol.40 , pp. 258-266
    • Mroginski, M.A.1    Murgida, D.H.2    Hildebrandt, P.3
  • 9
    • 50249177040 scopus 로고    scopus 로고
    • Heteronuclear NMR investigation on the structure and dynamics of the chromophore binding pocket of the cyanobacterial phytochrome Cph1
    • Hahn J, Strauss HM, Schmieder P (2008) Heteronuclear NMR investigation on the structure and dynamics of the chromophore binding pocket of the cyanobacterial phytochrome Cph1. J Am Chem Soc 130:11170-11178.
    • (2008) J Am Chem Soc , vol.130 , pp. 11170-11178
    • Hahn, J.1    Strauss, H.M.2    Schmieder, P.3
  • 10
    • 55749110269 scopus 로고    scopus 로고
    • Light-induced chromophore activity and signal transduction in phytochromes observed by 13C and 15N magic-angle spinning NMR
    • Rohmer T, et al. (2008) Light-induced chromophore activity and signal transduction in phytochromes observed by 13C and 15N magic-angle spinning NMR. Proc Natl Acad Sci USA 105:15229-15234.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15229-15234
    • Rohmer, T.1
  • 11
    • 12144264399 scopus 로고    scopus 로고
    • Light-induced conformational changes of cyanobacterial phytochrome Cph1 probed by limited proteolysis and autophosphorylation
    • DOI 10.1021/bi0484365
    • Esteban B, Carrascal M, Abian J, Lamparter T (2005) Light-induced conformational changes of cyanobacterial phytochrome Cph1 probed by limited proteolysis and autophosphorylation. Biochemistry 44:450-461. (Pubitemid 40105475)
    • (2005) Biochemistry , vol.44 , Issue.2 , pp. 450-461
    • Esteban, B.1    Carrascal, M.2    Abian, J.3    Lamparter, T.4
  • 12
    • 55749108880 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: Photoconversion and signal transduction
    • Yang X, Kuk J, Moffat K (2008) Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: Photoconversion and signal transduction. Proc Natl Acad Sci USA 105:14715-14720.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14715-14720
    • Yang, X.1    Kuk, J.2    Moffat, K.3
  • 13
    • 55749108535 scopus 로고    scopus 로고
    • The structure of a complete phytochrome sensory module in the Pr ground state
    • Essen LO, Mailliet J, Hughes J (2008) The structure of a complete phytochrome sensory module in the Pr ground state. Proc Natl Acad Sci USA 105:14709-14714.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14709-14714
    • Essen, L.O.1    Mailliet, J.2    Hughes, J.3
  • 14
    • 34547628072 scopus 로고    scopus 로고
    • Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion
    • DOI 10.1073/pnas.0701737104
    • Yang X, Stojkovic EA, Kuk J, Moffat K (2007) 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. (Pubitemid 47206179)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.30 , pp. 12571-12576
    • Yang, X.1    Stojkovic, E.A.2    Kuk, J.3    Moffat, K.4
  • 16
    • 0037418282 scopus 로고    scopus 로고
    • The pair of bacteriophytochromes from Agrobacterium tumefaciens are histidine kinases with opposing photobiological properties
    • DOI 10.1073/pnas.0437914100
    • Karniol B, Vierstra RD (2003) The pair of bacteriophytochromes from Agrobacterium tumefaciens are histidine kinases with opposing photobiological properties. Proc Natl Acad Sci USA 100:2807-2812. (Pubitemid 36297580)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.5 , pp. 2807-2812
    • Karniol, B.1    Vierstra, R.D.2
  • 17
    • 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 JR, et al. (2008) 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) J Biol Chem , vol.283 , pp. 12212-12226
    • Wagner, J.R.1
  • 19
    • 52949096101 scopus 로고    scopus 로고
    • Solution structure of a cyanobacterial phytochrome GAF domain in the red-light-absorbing ground state
    • Cornilescu G, Ulijasz AT, Cornilescu CC, Markley JL, VierstraRD(2008) Solution structure of a cyanobacterial phytochrome GAF domain in the red-light-absorbing ground state. J Mol Biol 383:403-413.
    • (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
  • 20
    • 10644265997 scopus 로고    scopus 로고
    • Harnessing phytochrome's glowing potential
    • Fischer AJ, Lagarias JC (2004) Harnessing phytochrome's glowing potential. Proc Natl Acad Sci USA 101:17334-17339.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17334-17339
    • Fischer, A.J.1    Lagarias, J.C.2
  • 21
    • 34548309457 scopus 로고    scopus 로고
    • Light-independent phytochrome signaling mediated by dominant GAF domain tyrosine mutants of Arabidopsis phytochromes in transgenic plants
    • Su YS, Lagarias JC (2007) Light-independent phytochrome signaling mediated by dominant GAF domain tyrosine mutants of Arabidopsis phytochromes in transgenic plants. Plant Cell 19:2124-2139.
    • (2007) Plant Cell , vol.19 , pp. 2124-2139
    • Su, Y.S.1    Lagarias, J.C.2
  • 22
    • 27944447344 scopus 로고    scopus 로고
    • Multiple roles of a conserved GAF domain tyrosine residue in cyanobacterial and plant phytochromes
    • Fischer AJ, et al. (2005) Multiple roles of a conserved GAF domain tyrosine residue in cyanobacterial and plant phytochromes. Biochemistry 44:15203-15215.
    • (2005) Biochemistry , vol.44 , pp. 15203-15215
    • Fischer, A.J.1
  • 23
    • 0027240608 scopus 로고
    • Ultrafast pump-probe spectroscopy of native etiolated oat phytochrome
    • Savikhin S, Wells T, Song PS, Struve WS (1993) Ultrafast pump-probe spectroscopy of native etiolated oat phytochrome. Biochemistry 32:7512-7518. (Pubitemid 23232326)
    • (1993) Biochemistry , vol.32 , Issue.29 , pp. 7512-7518
    • Savikhin, S.1    Wells, T.2    Song, P.-S.3    Struve, W.S.4
  • 24
    • 0030062964 scopus 로고    scopus 로고
    • Mechanism of native oat phytochrome photoreversion: A time-resolved absorption investigation
    • DOI 10.1021/bi952115z
    • Chen E, Lapko VN, Lewis JW, Song PS, Kliger DS (1996) Mechanism of native oat phytochrome photoreversion: A time-resolved absorption investigation. Biochemistry 35:843-850. (Pubitemid 26034568)
    • (1996) Biochemistry , vol.35 , Issue.3 , pp. 843-850
    • Chen, E.1    Lapko, V.N.2    Lewis, J.W.3    Song, P.-S.4    Kliger, D.S.5
  • 25
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger TC (2000) Maximum-likelihood density modification. Acta Crystallogr D 56:965-972.
    • (2000) Acta Crystallogr D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 27
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger AT, Adams PD, Clore M, Delano WL (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D 54:905-921.
    • (1998) Acta Crystallogr D , vol.54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.D.2    Clore, M.3    Delano, W.L.4
  • 28
    • 16644364842 scopus 로고    scopus 로고
    • REFMAC5dictionary: Organization of prior chemical knowledge and guidelines for its use
    • Vagin AA, et al. (2004)REFMAC5dictionary: Organization of prior chemical knowledge and guidelines for its use. Acta Crystallogr D 60:2184-2195.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2184-2195
    • Vagin, A.A.1
  • 29
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D 58:1948-1954.
    • (2002) Acta Crystallogr D , vol.58 , pp. 1948-1954
    • Adams, P.D.1


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