메뉴 건너뛰기




Volumn 61, Issue 1, 1999, Pages 11-21

Structural predictions on the 33 kDa extrinsic protein associated to the oxygen evolving complex of photosynthetic organisms

Author keywords

Manganese stabilizing protein; Oxygen evolution; Photosystem II; Protein structure prediction; PsbO protein

Indexed keywords

ALGA; CYANOBACTERIUM; MEMBRANE PROTEIN; PHOTOSYNTHESIS; PLANT; PROTEIN STRUCTURE;

EID: 0032703843     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006265816104     Document Type: Article
Times cited : (29)

References (36)
  • 1
    • 0028907510 scopus 로고
    • A quantitative secondary structure analysis of the 33 kDa extrinsic polypeptide of PS II by FTIR spectroscopy
    • Ahmed A, Tajmir-Riahi HA and Carpentie R (1995) A quantitative secondary structure analysis of the 33 kDa extrinsic polypeptide of PS II by FTIR spectroscopy. FEBS Lett 363: 65-68
    • (1995) FEBS Lett , vol.363 , pp. 65-68
    • Ahmed, A.1    Tajmir-Riahi, H.A.2    Carpentie, R.3
  • 3
    • 0029928973 scopus 로고    scopus 로고
    • Functional reconstitution of Photosystem II with recombinant manganese-stabilizing proteins containing mutations that remove the disulfide bridge
    • Betts SD, Ross JR, Hall KU, Pichersky E and Yocum CF (1996) Functional reconstitution of Photosystem II with recombinant manganese-stabilizing proteins containing mutations that remove the disulfide bridge. Biochim Biophys Acta 1274: 135-142
    • (1996) Biochim Biophys Acta , vol.1274 , pp. 135-142
    • Betts, S.D.1    Ross, J.R.2    Hall, K.U.3    Pichersky, E.4    Yocum, C.F.5
  • 4
    • 0030611016 scopus 로고    scopus 로고
    • Mutation Val235Ala weakens binding of the 33 kDa manganese stabilizing protein of PS II to one of two sites
    • Betts SD, Ross JR, Pichersky E and Yocum CF (1997) Mutation Val235Ala weakens binding of the 33 kDa manganese stabilizing protein of PS II to one of two sites. Biochemistry 36: 4047-4053
    • (1997) Biochemistry , vol.36 , pp. 4047-4053
    • Betts, S.D.1    Ross, J.R.2    Pichersky, E.3    Yocum, C.F.4
  • 5
    • 0032491192 scopus 로고    scopus 로고
    • The carboxyl-terminal tripeptide of the manganese-stabilizing protein is required for quantitative assembly into Photosystem II and for high rates of oxygen evolution activity
    • Betts SD, Lydakis-Simantiris N, Ross JR and Yocum CF (1998) The carboxyl-terminal tripeptide of the manganese-stabilizing protein is required for quantitative assembly into Photosystem II and for high rates of oxygen evolution activity. Biochemistry 37: 14230-14236
    • (1998) Biochemistry , vol.37 , pp. 14230-14236
    • Betts, S.D.1    Lydakis-Simantiris, N.2    Ross, J.R.3    Yocum, C.F.4
  • 6
    • 0031853225 scopus 로고    scopus 로고
    • The structure and function of the 33 kDa extrinsic protein of Photosystem II: A critical assessment
    • Bricker TM and Franke LK (1998) The structure and function of the 33 kDa extrinsic protein of Photosystem II: A critical assessment. Photosynthesis Res 56: 157-173
    • (1998) Photosynthesis Res , vol.56 , pp. 157-173
    • Bricker, T.M.1    Franke, L.K.2
  • 7
    • 0028019013 scopus 로고
    • Role of disulfide linkage and putative intermolecular binding residues in the stability and binding of the extrinsic manganesestabilizing protein to the PS II reaction center
    • Burnap RL, Quian M, Shen J-R, Inoue Y and Sherman LA (1994) Role of disulfide linkage and putative intermolecular binding residues in the stability and binding of the extrinsic manganesestabilizing protein to the PS II reaction center. Biochemistry 33: 13712-13718
    • (1994) Biochemistry , vol.33 , pp. 13712-13718
    • Burnap, R.L.1    Quian, M.2    Shen, J.-R.3    Inoue, Y.4    Sherman, L.A.5
  • 8
    • 0002564682 scopus 로고
    • Chloride binding proteins: Mechanistic implications for the oxygen-evolving complex of PS II
    • Coleman WJ (1990) Chloride binding proteins: Mechanistic implications for the oxygen-evolving complex of PS II. Photosynthesis Res 23: 1-27
    • (1990) Photosynthesis Res , vol.23 , pp. 1-27
    • Coleman, W.J.1
  • 9
    • 0025814801 scopus 로고
    • Arginyl-glycylaspartic acid (RGD): A cell adhesion motif
    • D'Souza SE, Ginsberg MH and Plow EF (1991) Arginyl-glycylaspartic acid (RGD): A cell adhesion motif. Trends Biochem Sci 16: 246-250
    • (1991) Trends Biochem Sci , vol.16 , pp. 246-250
    • D'Souza, S.E.1    Ginsberg, M.H.2    Plow, E.F.3
  • 10
    • 0032549019 scopus 로고    scopus 로고
    • Intramolecular cross-linking of the extrinsic 33 kDa protein leads to loss of oxygen evolution but not its ability of binding to PS II and stabilization of the manganese cluster
    • Enami I, Kamo M, Ohta H, Takahashi S, Miura T, Kusayanagi M, Tanabe S, Kamei A, Motoki A, Hirano M, Tomo T and Satoh K (1998) Intramolecular cross-linking of the extrinsic 33 kDa protein leads to loss of oxygen evolution but not its ability of binding to PS II and stabilization of the manganese cluster. J Biol Chem 273: 4629-4634
    • (1998) J Biol Chem , vol.273 , pp. 4629-4634
    • Enami, I.1    Kamo, M.2    Ohta, H.3    Takahashi, S.4    Miura, T.5    Kusayanagi, M.6    Tanabe, S.7    Kamei, A.8    Motoki, A.9    Hirano, M.10    Tomo, T.11    Satoh, K.12
  • 11
    • 0029874551 scopus 로고    scopus 로고
    • Fold recognition using sequence-derived predictions
    • Fischer D and Eisenberg D (1996) Fold recognition using sequence-derived predictions. Protein Sci 5: 947-955
    • (1996) Protein Sci , vol.5 , pp. 947-955
    • Fischer, D.1    Eisenberg, D.2
  • 12
    • 0029050362 scopus 로고
    • Interaction of the 33 kDa extrinsic protein with PS II: Identification of domains on the 33 kDa protein that are shielded from NHS-biotinylation by PS II
    • Frankel LK and Bricker TM (1995) Interaction of the 33 kDa extrinsic protein with PS II: Identification of domains on the 33 kDa protein that are shielded from NHS-biotinylation by PS II. Biochemistry 34: 7492-7497
    • (1995) Biochemistry , vol.34 , pp. 7492-7497
    • Frankel, L.K.1    Bricker, T.M.2
  • 14
    • 0032554633 scopus 로고    scopus 로고
    • Conformational changes in the extrinsic manganese stabilizing protein can occur upon binding to the Photosystem II reaction center: An isotope editing and FT-IR study
    • Hutchison RS, Betts SD, Yocum CF and Barry BA (1998) Conformational changes in the extrinsic manganese stabilizing protein can occur upon binding to the Photosystem II reaction center: An isotope editing and FT-IR study. Biochemistry 37: 5643-5653
    • (1998) Biochemistry , vol.37 , pp. 5643-5653
    • Hutchison, R.S.1    Betts, S.D.2    Yocum, C.F.3    Barry, B.A.4
  • 15
    • 0033524432 scopus 로고    scopus 로고
    • Manganese stabilizing protein of Photosystem II isathermostable, natively unfolded polypeptide
    • Lydakis-Simantiris N, Hutchison RS, Betts SD, Barry BA and Yocum CF (1999) Manganese stabilizing protein of Photosystem II isathermostable, natively unfolded polypeptide. Biochemistry 38: 404-414
    • (1999) Biochemistry , vol.38 , pp. 404-414
    • Lydakis-Simantiris, N.1    Hutchison, R.S.2    Betts, S.D.3    Barry, B.A.4    Yocum, C.F.5
  • 17
    • 0032551771 scopus 로고    scopus 로고
    • Two regions of the Mn-stabilizing protein from Synechococcus elengatus that are involved in binding to Photosystem II complexes
    • Motoki A, Shimazu T, Hirano M and Katoh S (1998) Two regions of the Mn-stabilizing protein from Synechococcus elengatus that are involved in binding to Photosystem II complexes. Biochim Biophys Acta 1365: 492-502
    • (1998) Biochim Biophys Acta , vol.1365 , pp. 492-502
    • Motoki, A.1    Shimazu, T.2    Hirano, M.3    Katoh, S.4
  • 18
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson WR and Lipman DJ (1988) Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 85: 2444-2448
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 19
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost B and Sander C (1993) Prediction of protein secondary structure at better than 70% accuracy. J Mol Biol 232: 584-599
    • (1993) J Mol Biol , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 20
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B and Sander C (1994a) Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19: 55-72
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 21
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • Rost B and Sander C (1994b) Conservation and prediction of solvent accessibility in protein families. Proteins 20: 216-226
    • (1994) Proteins , vol.20 , pp. 216-226
    • Rost, B.1    Sander, C.2
  • 22
    • 0028158628 scopus 로고
    • PHD-an automatic mail server for protein secondary structure prediction
    • Rost B, Sander C and Schneider R (1994) PHD-an automatic mail server for protein secondary structure prediction. Comput Appl Biosc 10: 53-60
    • (1994) Comput Appl Biosc , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 23
    • 0031577260 scopus 로고    scopus 로고
    • Protein fold recognition by prediction-based threading
    • Rost B, Schneider R and Sander C (1997) Protein fold recognition by prediction-based threading. J Mol Biol 270: 471-480
    • (1997) J Mol Biol , vol.270 , pp. 471-480
    • Rost, B.1    Schneider, R.2    Sander, C.3
  • 24
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti E and Pierschbacher MD (1987) New perspectives in cell adhesion: RGD and integrins. Science 238: 491-497
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 25
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N and Nei M (1987) The neighbor-joining method: A new method for reconstructing phylogenetic trees. Mol Biol Evol 4: 406-425
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 26
    • 0029966774 scopus 로고    scopus 로고
    • The extrinsic polypeptides of PS II
    • Seidler A (1996a) The extrinsic polypeptides of PS II. Biochim Biophys Acta 1277: 35-60
    • (1996) Biochim Biophys Acta , vol.1277 , pp. 35-60
    • Seidler, A.1
  • 27
    • 0030437746 scopus 로고    scopus 로고
    • Intermolecular and intramolecular interactions of the 33 kDa protein in PS II
    • Seidler A (1996b) Intermolecular and intramolecular interactions of the 33 kDa protein in PS II. Eur J Biochem 242: 485-490
    • (1996) Eur J Biochem , vol.242 , pp. 485-490
    • Seidler, A.1
  • 28
    • 0029831349 scopus 로고    scopus 로고
    • The role of the extrinsic 33kDa protein in Ca2+ binding in Photosystem II
    • Seidler A and Rutherford W (1996) The role of the extrinsic 33kDa protein in Ca2+ binding in Photosystem II. Biochemistry 35: 12104-12110
    • (1996) Biochemistry , vol.35 , pp. 12104-12110
    • Seidler, A.1    Rutherford, W.2
  • 29
    • 0030128825 scopus 로고    scopus 로고
    • On the role of the N-terminus of the extrinsic 33 kDa protein of PS II
    • Seidler A, Rutherford W and Michel H (1996) On the role of the N-terminus of the extrinsic 33 kDa protein of PS II. Plant Mol Biol 31: 183-188
    • (1996) Plant Mol Biol , vol.31 , pp. 183-188
    • Seidler, A.1    Rutherford, W.2    Michel, H.3
  • 30
    • 0030943887 scopus 로고    scopus 로고
    • Analysis of pH-induced structural changes of the isolated extrinsic 33 kilodalton protein of PS II
    • Shutova T, Irrgang K-D, Shubin V, Klimov VV and Renger G (1997) Analysis of pH-induced structural changes of the isolated extrinsic 33 kilodalton protein of PS II. Biochemistry 36: 6350-6358
    • (1997) Biochemistry , vol.36 , pp. 6350-6358
    • Shutova, T.1    Irrgang, K.-D.2    Shubin, V.3    Klimov, V.V.4    Renger, G.5
  • 31
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG and Gibson TJ (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acid Res 22: 4673-4680
    • (1994) Nucleic Acid Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 32
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F and Higgins DG (1997) The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acid Res 25: 4876-4882
    • (1997) Nucleic Acid Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 33
    • 0028568020 scopus 로고
    • Secondary structure of the 33kDa, extrinsic protein of PS II: A far-UV circular dichroism study
    • Xu Q, Nelson J and Bricker TM (1994) Secondary structure of the 33kDa, extrinsic protein of PS II: a far-UV circular dichroism study. Biochim Biophys Acta 1188: 427-431
    • (1994) Biochim Biophys Acta , vol.1188 , pp. 427-431
    • Xu, Q.1    Nelson, J.2    Bricker, T.M.3
  • 34
    • 0010131239 scopus 로고
    • An FTIR study of calcium interactions in Photosystem II
    • Mathis P (ed). Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Zhang HM, Fischer G and Wydrznski T (1995) An FTIR study of calcium interactions in Photosystem II. In: Mathis P (ed) Photosynthesis: From Light to Biosphere, Vol II, pp 447-450. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • (1995) Photosynthesis: From Light to Biosphere , vol.2 , pp. 447-450
    • Zhang, H.M.1    Fischer, G.2    Wydrznski, T.3
  • 35
    • 0029959862 scopus 로고    scopus 로고
    • Fluorescence and Fourier-transform infrared spectroscopic studies on the role of disulfide bond in the calcium binding in the 33 kDa protein of Photosystem II
    • Zhang L-X, Liang H-G, Wang J, Li WR and Yu TZ (1996) Fluorescence and Fourier-transform infrared spectroscopic studies on the role of disulfide bond in the calcium binding in the 33 kDa protein of Photosystem II. Photosynth Res 48: 379-384
    • (1996) Photosynth Res , vol.48 , pp. 379-384
    • Zhang, L.-X.1    Liang, H.-G.2    Wang, J.3    Li, W.R.4    Yu, T.Z.5
  • 36
    • 0032578473 scopus 로고    scopus 로고
    • Hydrodynamic studies on the manganese-stabilizing protein of Photosystem II
    • Zubrzycki IZ, Franke LK, Russo PS and Bricker TM (1998) Hydrodynamic studies on the manganese-stabilizing protein of Photosystem II. Biochemistry 37: 13553-13558
    • (1998) Biochemistry , vol.37 , pp. 13553-13558
    • Zubrzycki, I.Z.1    Franke, L.K.2    Russo, P.S.3    Bricker, T.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.