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Volumn 350, Issue 5, 2005, Pages 1051-1060

The 1.49 Å resolution crystal structure of PsbQ from photosystem II of Spinacia oleracea reveals a PPII structure in the N-terminal region

Author keywords

Photosystem II; PPII; Protein structure; PsbQ

Indexed keywords

CARBONYL DERIVATIVE; PROLINE; PROTEIN; PROTEIN PSBQ; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; PEPTIDE; POLYPROLINE; VEGETABLE PROTEIN; WATER; ZINC;

EID: 21744439800     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.05.044     Document Type: Article
Times cited : (58)

References (48)
  • 1
    • 0037295369 scopus 로고    scopus 로고
    • Photosystem II: The engine of life
    • J. Barber Photosystem II: the engine of life Quart. Rev. Biophys. 36 2003 71 89
    • (2003) Quart. Rev. Biophys. , vol.36 , pp. 71-89
    • Barber, J.1
  • 2
    • 0037195306 scopus 로고    scopus 로고
    • Photosystem II and photosynthetic oxidation of water: An overview
    • C. Goussias, A. Boussac, and A.W. Rutherford Photosystem II and photosynthetic oxidation of water: an overview Phil. Trans. Roy. Soc. ser. B 357 2002 1369 1381 discussion 1419-1420
    • (2002) Phil. Trans. Roy. Soc. Ser. B , vol.357 , pp. 1369-1381
    • Goussias, C.1    Boussac, A.2    Rutherford, A.W.3
  • 3
    • 0036412420 scopus 로고    scopus 로고
    • Chloride and calcium in Photosystem II: From effects to enigma
    • P.H. Homann Chloride and calcium in Photosystem II: from effects to enigma Photosynth. Res. 73 2002 169 175
    • (2002) Photosynth. Res. , vol.73 , pp. 169-175
    • Homann, P.H.1
  • 4
    • 0042360203 scopus 로고    scopus 로고
    • Period-four oscillations of the flash-induced oxygen formation in photosynthesis
    • P. Joliot Period-four oscillations of the flash-induced oxygen formation in photosynthesis Photosynth. Res. 76 2003 65 72
    • (2003) Photosynth. Res. , vol.76 , pp. 65-72
    • Joliot, P.1
  • 5
    • 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, and P. Orth Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution Nature 409 2001 739 743
    • (2001) Nature , vol.409 , 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
  • 6
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7 Å resolution
    • N. Kamiya, and J.R. Shen Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7 Å resolution Proc. Natl Acad. Sci. USA 100 2003 98 103
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.R.2
  • 9
    • 0037195337 scopus 로고    scopus 로고
    • Organization of transmembrane helices in photosystem II: Comparison of plants and cyanobacteria
    • J. Barber, and J. Nield Organization of transmembrane helices in photosystem II: comparison of plants and cyanobacteria Phil. Trans. Roy. Soc. ser. B 357 2002 1329 1335
    • (2002) Phil. Trans. Roy. Soc. Ser. B , vol.357 , pp. 1329-1335
    • Barber, J.1    Nield, J.2
  • 11
    • 12244313729 scopus 로고    scopus 로고
    • Binding and functional properties of the extrinsic proteins in oxygen-evolving photosystem II particle from a green alga, Chlamydomonas reinhardtii having His-tagged CP47
    • T. Suzuki, J. Minagawa, T. Tomo, K. Sonoike, H. Ohta, and I. Enami Binding and functional properties of the extrinsic proteins in oxygen-evolving photosystem II particle from a green alga, Chlamydomonas reinhardtii having His-tagged CP47 Plant Cell Physiol. 44 2003 76 84
    • (2003) Plant Cell Physiol. , vol.44 , pp. 76-84
    • Suzuki, T.1    Minagawa, J.2    Tomo, T.3    Sonoike, K.4    Ohta, H.5    Enami, I.6
  • 12
    • 0036013399 scopus 로고    scopus 로고
    • Comparison of the structure of the extrinsic 33 kDa protein from different organisms
    • A. Tohri, T. Suzuki, S. Okuyama, K. Kamino, A. Motoki, and M. Hirano Comparison of the structure of the extrinsic 33 kDa protein from different organisms Plant Cell Physiol. 43 2002 429 439
    • (2002) Plant Cell Physiol. , vol.43 , pp. 429-439
    • Tohri, A.1    Suzuki, T.2    Okuyama, S.3    Kamino, K.4    Motoki, A.5    Hirano, M.6
  • 13
    • 0034489364 scopus 로고    scopus 로고
    • Cross-reconstitution of various extrinsic proteins and photosystem II complexes from cyanobacteria, red algae and higher plants
    • I. Enami, S. Yoshihara, A. Tohri, A. Okumura, H. Ohta, and J.R. Shen Cross-reconstitution of various extrinsic proteins and photosystem II complexes from cyanobacteria, red algae and higher plants Plant Cell Physiol. 41 2000 1354 1364
    • (2000) Plant Cell Physiol. , vol.41 , pp. 1354-1364
    • Enami, I.1    Yoshihara, S.2    Tohri, A.3    Okumura, A.4    Ohta, H.5    Shen, J.R.6
  • 14
    • 0029966774 scopus 로고    scopus 로고
    • The extrinsic polypeptides of photosystem II
    • A. Seidler The extrinsic polypeptides of photosystem II Biochim. Biophys. Acta 1277 1996 35 60
    • (1996) Biochim. Biophys. Acta , vol.1277 , pp. 35-60
    • Seidler, A.1
  • 15
    • 0742305590 scopus 로고    scopus 로고
    • Evolution of oxygenic photosynthesis: Genome-wide analysis of the OEC extrinsic proteins
    • J. De Las Rivas, M. Balsera, and J. Barber Evolution of oxygenic photosynthesis: genome-wide analysis of the OEC extrinsic proteins Trends Plant Sci. 9 2004 18 25
    • (2004) Trends Plant Sci. , vol.9 , pp. 18-25
    • De Las Rivas, J.1    Balsera, M.2    Barber, J.3
  • 16
    • 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, and I. Enami Extrinsic proteins of photosystem II: an intermediate member of PsbQ protein family in red algal PS II Eur. J. Biochem. 270 2003 4156 4163
    • (2003) Eur. J. Biochem. , vol.270 , 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
  • 17
    • 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, and 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 41 2002 8004 8012
    • (2002) Biochemistry , vol.41 , 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
  • 18
    • 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, and 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 16 2004 2164 2175
    • (2004) Plant Cell , vol.16 , pp. 2164-2175
    • Thornton, L.E.1    Ohkawa, H.2    Roose, J.L.3    Kashino, Y.4    Keren, N.5    Pakrasi, H.B.6
  • 19
    • 2442543556 scopus 로고    scopus 로고
    • Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum
    • K. Ifuku, T. Nakatsu, H. Kato, and F. Sato Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum EMBO Rep. 5 2004 362 367
    • (2004) EMBO Rep. , vol.5 , pp. 362-367
    • Ifuku, K.1    Nakatsu, T.2    Kato, H.3    Sato, F.4
  • 21
    • 0034711009 scopus 로고    scopus 로고
    • Conformational changes in photosystem II supercomplexes upon removal of extrinsic subunits
    • E.J. Boekema, J.F. van Breemen, H. van Roon, and J.P. Dekker Conformational changes in photosystem II supercomplexes upon removal of extrinsic subunits Biochemistry 39 2000 12907 12915
    • (2000) Biochemistry , vol.39 , pp. 12907-12915
    • Boekema, E.J.1    Van Breemen, J.F.2    Van Roon, H.3    Dekker, J.P.4
  • 22
    • 0032032367 scopus 로고    scopus 로고
    • Localization of the 23-kDa subunit of the oxygen-evolving complex of photosystem II by electron microscopy
    • E.J. Boekema, J. Nield, B. Hankamer, and J. Barber Localization of the 23-kDa subunit of the oxygen-evolving complex of photosystem II by electron microscopy Eur. J. Biochem. 252 1998 268 276
    • (1998) Eur. J. Biochem. , vol.252 , pp. 268-276
    • Boekema, E.J.1    Nield, J.2    Hankamer, B.3    Barber, J.4
  • 23
    • 0033989509 scopus 로고    scopus 로고
    • 3D map of the plant photosystem II supercomplex obtained by cryoelectron microscopy and single particle analysis
    • J. Nield, E.V. Orlova, E.P. Morris, B. Gowen, M. van Heel, and J. Barber 3D map of the plant photosystem II supercomplex obtained by cryoelectron microscopy and single particle analysis Nature Struct. Biol. 7 2000 44 47
    • (2000) Nature Struct. Biol. , vol.7 , pp. 44-47
    • Nield, J.1    Orlova, E.V.2    Morris, E.P.3    Gowen, B.4    Van Heel, M.5    Barber, J.6
  • 24
    • 0037177852 scopus 로고    scopus 로고
    • Three-dimensional electron cryo-microscopy study of the extrinsic domains of the oxygen-evolving complex of spinach: Assignment of the PsbO protein
    • J. Nield, M. Balsera, J. De Las Rivas, and J. Barber Three-dimensional electron cryo-microscopy study of the extrinsic domains of the oxygen-evolving complex of spinach: assignment of the PsbO protein J. Biol. Chem. 277 2002 15006 15012
    • (2002) J. Biol. Chem. , vol.277 , pp. 15006-15012
    • Nield, J.1    Balsera, M.2    De Las Rivas, J.3    Barber, J.4
  • 25
    • 0141592329 scopus 로고    scopus 로고
    • The single tryptophan of the PsbQ protein of photosystem II is at the end of a 4-α-helical bundle domain
    • M. Balsera, J.B. Arellano, F. Pazos, D. Devos, A. Valencia, and J. De Las Rivas The single tryptophan of the PsbQ protein of photosystem II is at the end of a 4-α-helical bundle domain Eur. J. Biochem. 270 2003 3916 3927
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3916-3927
    • Balsera, M.1    Arellano, J.B.2    Pazos, F.3    Devos, D.4    Valencia, A.5    De Las Rivas, J.6
  • 26
    • 0037417759 scopus 로고    scopus 로고
    • 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, and 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 42 2003 1000 1007
    • (2003) Biochemistry , vol.42 , pp. 1000-1007
    • Balsera, M.1    Arellano, J.B.2    Gutierrez, J.R.3    Heredia, P.4    Revuelta, J.L.5    De Las Rivas, J.6
  • 27
    • 0001628742 scopus 로고
    • Partial degradation of the 18-kDa protein of the photosynthetic oxygen-evolving complex - A study of a binding-site
    • T. Kuwabara, T. Murata, M. Miyao, and N. Murata Partial degradation of the 18-kDa protein of the photosynthetic oxygen-evolving complex - a study of a binding-site Biochim. Biophys. Acta 850 1986 146 155
    • (1986) Biochim. Biophys. Acta , vol.850 , pp. 146-155
    • Kuwabara, T.1    Murata, T.2    Miyao, M.3    Murata, N.4
  • 28
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K.A. Sharp, and B. Honig Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins: Struct. Funct. Genet. 11 1991 281 296
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 29
    • 0018781196 scopus 로고
    • Isoelectric points of spinach thylakoid membrane surfaces as determined by cross partition
    • H.E. Akerlund, B. Andersson, A. Persson, and P. Albertsson Isoelectric points of spinach thylakoid membrane surfaces as determined by cross partition Biochim. Biophys. Acta 552 1979 238 246
    • (1979) Biochim. Biophys. Acta , vol.552 , pp. 238-246
    • Akerlund, H.E.1    Andersson, B.2    Persson, A.3    Albertsson, P.4
  • 30
    • 0032980562 scopus 로고    scopus 로고
    • A survey of left-handed polyproline II helices
    • B.J. Stapley, and T.P. Creamer A survey of left-handed polyproline II helices Protein Sci. 8 1999 587 595
    • (1999) Protein Sci. , vol.8 , pp. 587-595
    • Stapley, B.J.1    Creamer, T.P.2
  • 33
    • 1642580518 scopus 로고    scopus 로고
    • Protein assembly of photosystem II and accumulation of subcomplexes in the absence of low molecular mass subunits PsbL and PsbJ
    • M. Suorsa, R.E. Regel, V. Paakkarinen, N. Battchikova, R.G. Herrmann, and E.M. Aro Protein assembly of photosystem II and accumulation of subcomplexes in the absence of low molecular mass subunits PsbL and PsbJ Eur. J. Biochem. 271 2004 96 107
    • (2004) Eur. J. Biochem. , vol.271 , pp. 96-107
    • Suorsa, M.1    Regel, R.E.2    Paakkarinen, V.3    Battchikova, N.4    Herrmann, R.G.5    Aro, E.M.6
  • 34
    • 0026610823 scopus 로고
    • Characterization of a prolyl endopeptidase from spinach thylakoids
    • T. Kuwabara Characterization of a prolyl endopeptidase from spinach thylakoids FEBS Letters 300 1992 127 130
    • (1992) FEBS Letters , vol.300 , pp. 127-130
    • Kuwabara, T.1
  • 35
    • 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, and M. Sudol The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains FASEB J. 14 2000 231 238
    • (2000) FASEB J. , vol.14 , pp. 231-238
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 36
    • 0030008366 scopus 로고    scopus 로고
    • Copper(II)-catalyzed amide isomerization: Evidence for N-coordination
    • C. Cox, D. Ferraris, N.N. Murthy, and T. Lectka Copper(II)-catalyzed amide isomerization: evidence for N-coordination J. Am. Chem. Soc. 118 1996 5332 5333
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5332-5333
    • Cox, C.1    Ferraris, D.2    Murthy, N.N.3    Lectka, T.4
  • 37
    • 0141648140 scopus 로고    scopus 로고
    • Binding of copper(II) ions to the polyproline II helices of PEVK modules of the giant elastic protein titin as revealed by ESI-MS, CD and NMR
    • K. Ma, and K. Wang Binding of copper(II) ions to the polyproline II helices of PEVK modules of the giant elastic protein titin as revealed by ESI-MS, CD and NMR Biopolymers 70 2003 297 309
    • (2003) Biopolymers , vol.70 , pp. 297-309
    • Ma, K.1    Wang, K.2
  • 39
    • 0037126686 scopus 로고    scopus 로고
    • Proline cis-trans isomerization and protein folding
    • W.J. Wedemeyer, E. Welker, and H.A. Scheraga Proline cis-trans isomerization and protein folding Biochemistry 41 2002 14637 14644
    • (2002) Biochemistry , vol.41 , pp. 14637-14644
    • Wedemeyer, W.J.1    Welker, E.2    Scheraga, H.A.3
  • 40
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project Number 4
    • Collaborative Computing Project Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 41
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallog. sect. A 50 1994 157 163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 43
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron-density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 44
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallog. sect. D 53 1997 240 255
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 45
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • M.D. Winn, M.N. Isupov, and G.N. Murshudov Use of TLS parameters to model anisotropic displacements in macromolecular refinement Acta Crystallog. sect. D 57 2001 122 133
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 47
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsh, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsh, W.1    Sander, C.2
  • 48
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J.D. Thompson, T.J. Gibson, F. Plewniak, F. Jeanmougin, and D.G. Higgins The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucl. Acids Res. 25 1997 4876 4882
    • (1997) Nucl. Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5


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