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Volumn 4, Issue 12, 2005, Pages 1003-1010

Structure and evolution of the extrinsic proteins that stabilize the oxygen-evolving engine

Author keywords

[No Author keywords available]

Indexed keywords

MANGANESE; OXYGEN; PROTEIN;

EID: 29144456629     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/b506874f     Document Type: Article
Times cited : (27)

References (31)
  • 1
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the photosynthetic oxygen-evolving centre
    • K. N. Ferreira T. M. Iverson K. Maghlaoui J. Barber S. Iwata Architecture of the photosynthetic oxygen-evolving centre Science 2004 303 5665 1831-8.
    • (2004) Science , vol.303 , Issue.5665 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 2
    • 4143120197 scopus 로고    scopus 로고
    • Structure of photosystem II and molecular architecture of the oxygen-evolving centre
    • S. Iwata J. Barber Structure of photosystem II and molecular architecture of the oxygen-evolving centre Curr. Opin. Struct. Biol. 2004 14 4 447-53.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , Issue.4 , pp. 447-453
    • Iwata, S.1    Barber, J.2
  • 3
    • 0742305590 scopus 로고    scopus 로고
    • Evolution of oxygenic photosynthesis: Genome-wide analysis of the OEC extrinsic proteins
    • J. De Las Rivas M. Balsera J. Barber Evolution of oxygenic photosynthesis: genome-wide analysis of the OEC extrinsic proteins Trends Plant Sci. 2004 9 1 18-25.
    • (2004) Trends Plant Sci. , vol.9 , Issue.1 , pp. 18-25
    • De Las Rivas, J.1    Balsera, M.2    Barber, J.3
  • 4
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • A. Zouni H. T. Witt J. Kern P. Fromme N. Krauss W. Saenger P. Orth Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution Nature 2001 409 6821 739-43.
    • (2001) Nature , vol.409 , Issue.6821 , pp. 739-743
    • Zouni, A.1    Witt, H.T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7
  • 5
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Å resolution
    • N. Kamiya J. R. Shen Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Å resolution Proc. Natl. Acad. Sci. U. S. A. 2003 100 1 98-103.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , Issue.1 , pp. 98-103
    • Kamiya, N.1    Shen, J.R.2
  • 6
    • 18644372534 scopus 로고    scopus 로고
    • Functional implications on the mechanism of the function of photosystem II including water oxidation based on the structure of photosystem II
    • P. Fromme J. Kern B. Loll J. Biesiadka W. Saenger H. T. Witt N. Krauss A. Zouni Functional implications on the mechanism of the function of photosystem II including water oxidation based on the structure of photosystem II Philos. Trans. R. Soc. London, Ser. B 2002 357 1426 1337-44.
    • (2002) Philos. Trans. R. Soc. London, Ser. B , vol.357 , Issue.1426 , pp. 1337-1344
    • Fromme, P.1    Kern, J.2    Loll, B.3    Biesiadka, J.4    Saenger, W.5    Witt, H.T.6    Krauss, N.7    Zouni, A.8
  • 8
    • 0042568828 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic studies on the extrinsic 23 kDa protein in the oxygen-evolving complex of photosystem II
    • K. Ifuku T. Nakatsu H. Kato F. Sato Crystallization and preliminary crystallographic studies on the extrinsic 23 kDa protein in the oxygen-evolving complex of photosystem II Acta Crystallogr., Sect. D: Biol. Crystallogr. 2003 59 Pt 8 1462-3.
    • (2003) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.59 , pp. 1462-1463
    • Ifuku, K.1    Nakatsu, T.2    Kato, H.3    Sato, F.4
  • 9
    • 21744439800 scopus 로고    scopus 로고
    • The 1.49 Å resolution crystal structure of PsbQ from photosystem II of Spinacia oleracea reveals a PPII structure in the N-terminal region
    • M. Balsera J. B. Arellano J. L. Revuelta J. De Las Rivas J. A. Hermoso The 1.49 Å resolution crystal structure of PsbQ from photosystem II of Spinacia oleracea reveals a PPII structure in the N-terminal region J. Mol. Biol. 2005 359 5 1051-60.
    • (2005) J. Mol. Biol. , vol.359 , Issue.5 , pp. 1051-1060
    • Balsera, M.1    Arellano, J.B.2    Revuelta, J.L.3    De Las Rivas, J.4    Hermoso, J.A.5
  • 11
    • 0028177080 scopus 로고
    • A simulation comparison of phylogeny algorithms under equal and unequal evolutionary rates
    • M. K. Kuhner J. Felsenstein A simulation comparison of phylogeny algorithms under equal and unequal evolutionary rates Mol. Biol. Evol. 1994 11 3 459-68.
    • (1994) Mol. Biol. Evol. , vol.11 , Issue.3 , pp. 459-468
    • Kuhner, M.K.1    Felsenstein, J.2
  • 12
    • 0033756316 scopus 로고    scopus 로고
    • Maximum likelihood estimation of recombination rates from population data
    • M. K. Kuhner J. Yamato J. Felsenstein Maximum likelihood estimation of recombination rates from population data Genetics 2000 156 3 1393-401.
    • (2000) Genetics , vol.156 , Issue.3 , pp. 1393-1401
    • Kuhner, M.K.1    Yamato, J.2    Felsenstein, J.3
  • 13
    • 0037172810 scopus 로고    scopus 로고
    • Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides
    • Y. Kashino W. M. Lauber J. A. Carroll Q. Wang J. Whitmarsh K. Satoh H. B. Pakrasi Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides Biochemistry 2002 41 25 8004-12.
    • (2002) Biochemistry , vol.41 , Issue.25 , pp. 8004-8012
    • Kashino, Y.1    Lauber, W.M.2    Carroll, J.A.3    Wang, Q.4    Whitmarsh, J.5    Satoh, K.6    Pakrasi, H.B.7
  • 14
    • 0142057153 scopus 로고    scopus 로고
    • Extrinsic proteins of photosystem II: An intermediate member of PsbQ protein family in red algal PS II
    • H. Ohta T. Suzuki M. Ueno A. Okumura S. Yoshihara J. R. Shen I. Enami Extrinsic proteins of photosystem II: an intermediate member of PsbQ protein family in red algal PS II Eur. J. Biochem. 2003 270 20 4156-63.
    • (2003) Eur. J. Biochem. , vol.270 , Issue.20 , pp. 4156-4163
    • Ohta, H.1    Suzuki, T.2    Ueno, M.3    Okumura, A.4    Yoshihara, S.5    Shen, J.R.6    Enami, I.7
  • 15
    • 18144430898 scopus 로고    scopus 로고
    • The Manganese-stabilizing Protein Is Required for Photosystem II Assembly/Stability and Photoautotrophy in Higher Plants
    • X. Yi M. McChargue S. Laborde L. K. Frankel T. M. Bricker The Manganese-stabilizing Protein Is Required for Photosystem II Assembly/Stability and Photoautotrophy in Higher Plants J. Biol. Chem. 2005 280 16 16170-4.
    • (2005) J. Biol. Chem. , vol.280 , Issue.16 , pp. 16170-16174
    • Yi, X.1    McChargue, M.2    Laborde, S.3    Frankel, L.K.4    Bricker, T.M.5
  • 16
    • 12144270027 scopus 로고    scopus 로고
    • PsbQ (Sll1638) in Synechocystis sp. PCC 6803 is required for photosystem II activity in specific mutants and in nutrient-limiting conditions
    • T. C. Summerfield J. A. Shand F. K. Bentley J. J. Eaton-Rye PsbQ (Sll1638) in Synechocystis sp. PCC 6803 is required for photosystem II activity in specific mutants and in nutrient-limiting conditions Biochemistry 2005 44 2 805-15.
    • (2005) Biochemistry , vol.44 , Issue.2 , pp. 805-815
    • Summerfield, T.C.1    Shand, J.A.2    Bentley, F.K.3    Eaton-Rye, J.J.4
  • 17
    • 4043148624 scopus 로고    scopus 로고
    • Homologs of plant PsbP and PsbQ proteins are necessary for regulation of photosystem II activity in the cyanobacterium Synechocystis 6803
    • L. E. Thornton H. Ohkawa J. L. Roose Y. Kashino N. Keren H. B. Pakrasi Homologs of plant PsbP and PsbQ proteins are necessary for regulation of photosystem II activity in the cyanobacterium Synechocystis 6803 Plant Cell 2004 16 8 2164-75.
    • (2004) Plant Cell , vol.16 , Issue.8 , pp. 2164-2175
    • Thornton, L.E.1    Ohkawa, H.2    Roose, J.L.3    Kashino, Y.4    Keren, N.5    Pakrasi, H.B.6
  • 18
    • 4043080672 scopus 로고    scopus 로고
    • Analysis of the structure of the PsbO protein and its implications
    • J. De Las Rivas J. Barber Analysis of the structure of the PsbO protein and its implications Photosynth. Res. 2004 81 329-343.
    • (2004) Photosynth. Res. , vol.81 , pp. 329-343
    • De Las Rivas, J.1    Barber, J.2
  • 22
    • 0032428150 scopus 로고    scopus 로고
    • A protein required for nuclear-protein import, Mog1p, directly interacts with GTP-Gsp1p, the Saccharomyces cerevisiae ran homologue
    • M. Oki T. Nishimoto A protein required for nuclear-protein import, Mog1p, directly interacts with GTP-Gsp1p, the Saccharomyces cerevisiae ran homologue Proc. Natl. Acad. Sci. U. S. A. 1998 95 26 15388-93.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , Issue.26 , pp. 15388-15393
    • Oki, M.1    Nishimoto, T.2
  • 23
    • 0034725707 scopus 로고    scopus 로고
    • The mammalian Mog1 protein is a guanine nucleotide release factor for Ran
    • S. M. Steggerda B. M. Paschal The mammalian Mog1 protein is a guanine nucleotide release factor for Ran J. Biol. Chem. 2000 275 30 23175-80.
    • (2000) J. Biol. Chem. , vol.275 , Issue.30 , pp. 23175-23180
    • Steggerda, S.M.1    Paschal, B.M.2
  • 24
    • 11144256226 scopus 로고    scopus 로고
    • Role for the Ran binding protein, Mog1p, in Saccharomyces cerevisiae SLN1-SKN7 signal transduction
    • J. M. Lu R. J. Deschenes J. S. Fassler Role for the Ran binding protein, Mog1p, in Saccharomyces cerevisiae SLN1-SKN7 signal transduction Eukaryotic Cell 2004 3 6 1544-56.
    • (2004) Eukaryotic Cell , vol.3 , Issue.6 , pp. 1544-1556
    • Lu, J.M.1    Deschenes, R.J.2    Fassler, J.S.3
  • 25
    • 0032991536 scopus 로고    scopus 로고
    • GTP bound to chloroplast thylakoid membranes is required for light-induced, multienzyme degradation of the photosystem II D1 protein
    • C. Spetea T. Hundal F. Lohmann B. Andersson GTP bound to chloroplast thylakoid membranes is required for light-induced, multienzyme degradation of the photosystem II D1 protein Proc. Natl. Acad. Sci. U. S. A. 1999 96 11 6547-52.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , Issue.11 , pp. 6547-6552
    • Spetea, C.1    Hundal, T.2    Lohmann, F.3    Andersson, B.4
  • 26
    • 0034629470 scopus 로고    scopus 로고
    • GTP enhances the degradation of the photosystem II D1 protein irrespective of its conformational heterogeneity at the Q(B) site
    • C. Spetea N. Keren T. Hundal J. M. Doan I. Ohad B. Andersson GTP enhances the degradation of the photosystem II D1 protein irrespective of its conformational heterogeneity at the Q(B) site J. Biol. Chem. 2000 275 10 7205-11.
    • (2000) J. Biol. Chem. , vol.275 , Issue.10 , pp. 7205-7211
    • Spetea, C.1    Keren, N.2    Hundal, T.3    Doan, J.M.4    Ohad, I.5    Andersson, B.6
  • 28
    • 0037417759 scopus 로고    scopus 로고
    • Rivas, Structural analysis of the PsbQ protein of photosystem II by Fourier transform infrared and circular dichroic spectroscopy and by bioinformatic methods
    • M. Balsera J. B. Arellano J. R. Gutierrez P. Heredia J. L. Revuelta J. De Las Rivas, Structural analysis of the PsbQ protein of photosystem II by Fourier transform infrared and circular dichroic spectroscopy and by bioinformatic methods Biochemistry 2003 42 4 1000-7.
    • (2003) Biochemistry , vol.42 , Issue.4 , pp. 1000-1007
    • Balsera, M.1    Arellano, J.B.2    Gutierrez, J.R.3    Heredia, P.4    Revuelta, J.L.5    De Las, J.6
  • 29
    • 0141592329 scopus 로고    scopus 로고
    • Rivas, The single tryptophan of the PsbQ protein of photosystem II is at the end of a 4-alpha-helical bundle domain
    • M. Balsera J. B. Arellano F. Pazos D. Devos A. Valencia J. De Las Rivas, The single tryptophan of the PsbQ protein of photosystem II is at the end of a 4-alpha-helical bundle domain Eur. J. Biochem. 2003 270 19 3916-27.
    • (2003) Eur. J. Biochem. , vol.270 , Issue.19 , pp. 3916-3927
    • Balsera, M.1    Arellano, J.B.2    Pazos, F.3    Devos, D.4    Valencia, A.5    De Las, J.6
  • 30
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • B. K. Kay M. P. Williamson M. Sudol The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains FASEB J. 2000 14 2 231-41.
    • (2000) FASEB J. , vol.14 , Issue.2 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 31
    • 0038183834 scopus 로고    scopus 로고
    • Synthetic inhibitors of proline-rich ligand-mediated protein–protein interaction: Potent analogs of UCS15A
    • C. Oneyama T. Agatsuma Y. Kanda H. Nakano S. V. Sharma S. Nakano F. Narazaki K. Tatsuta Synthetic inhibitors of proline-rich ligand-mediated protein–protein interaction: potent analogs of UCS15A Chem. Biol. 2003 10 5 443-51.
    • (2003) Chem. Biol. , vol.10 , Issue.5 , pp. 443-451
    • Oneyama, C.1    Agatsuma, T.2    Kanda, Y.3    Nakano, H.4    Sharma, S.V.5    Nakano, S.6    Narazaki, F.7    Tatsuta, K.8


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