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Volumn 81, Issue 3, 2004, Pages 227-237

Comparative analyses of three-dimensional models of bacterial reaction centers

Author keywords

bacteriochlorophyll; electron transfer; purple bacteria; Rhodobacter sphaeroides; X ray diffraction

Indexed keywords

BACTERIA (MICROORGANISMS); PROTEOBACTERIA; RHODOBACTER; RHODOBACTER SPHAEROIDES;

EID: 4043114976     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:PRES.0000036848.19334.45     Document Type: Review
Times cited : (11)

References (46)
  • 1
    • 85143312233 scopus 로고
    • Crystallization of reaction centers from Rhodobacter sphaeroides
    • Michel H (ed) CRC Press, Boca Raton, Florida
    • Allen JP and Feher G (1991) Crystallization of reaction centers from Rhodobacter sphaeroides. In: Michel H (ed) Crystallization of Membrane Proteins, pp 137-152. CRC Press, Boca Raton, Florida
    • (1991) Crystallization of Membrane Proteins , pp. 137-152
    • Allen, J.P.1    Feher, G.2
  • 2
    • 0023395661 scopus 로고
    • Structure of the reaction center from Rhodbacter sphaeroides R-26. The cofactors
    • Allen JP, Feher G, Yeates TO, Komiya H and Rees DC (1987) Structure of the reaction center from Rhodbacter sphaeroides R-26. The cofactors. Proc Natl Acad Sci USA 84: 5730-5734
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5730-5734
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 3
    • 0000840344 scopus 로고    scopus 로고
    • Structural homology of reaction centers from Rhodopseudomonas sphaeroides and Rhodopseudomonas viridis as determined by X-ray diffraction
    • Allen JP, Feher G, Yeates TO, Rees DC, Deisenhofer J, Michel H and Huber R (1996) Structural homology of reaction centers from Rhodopseudomonas sphaeroides and Rhodopseudomonas viridis as determined by X-ray diffraction, Proc Natl Acad Sci USA 83: 8589-8593
    • (1996) Proc Natl Acad Sci USA , vol.83 , pp. 8589-8593
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Rees, D.C.4    Deisenhofer, J.5    Michel, H.6    Huber, R.7
  • 4
    • 0029140387 scopus 로고
    • Structure of the photochemical reaction center of a spheroidene containing purple bacterium, Rhodobacter sphaeroides Y, at 3 Å resolution
    • Arnoux B, Gaucher JF, Ducruix A and Reiss-Husson F (1995) Structure of the photochemical reaction center of a spheroidene containing purple bacterium, Rhodobacter sphaeroides Y, at 3 Å resolution. Acta Crystallogr D 51: 368-379
    • (1995) Acta Crystallogr D , vol.51 , pp. 368-379
    • Arnoux, B.1    Gaucher, J.F.2    Ducruix, A.3    Reiss-Husson, F.4
  • 7
    • 0034244556 scopus 로고    scopus 로고
    • Membrane proteins: Are we destined to repeat history
    • Bowie JU (2001) Membrane proteins: are we destined to repeat history. Curr Opin Struc Biol 10: 435-437
    • (2001) Curr Opin Struc Biol , vol.10 , pp. 435-437
    • Bowie, J.U.1
  • 9
    • 0026597444 scopus 로고
    • Free R-value - A novel statistical quantity for assessing the accuracy of crystal-structures
    • Brünger AT (1992) Free R-value - a novel statistical quantity for assessing the accuracy of crystal-structures. Nature 335: 472-475
    • (1992) Nature , vol.335 , pp. 472-475
    • Brünger, A.T.1
  • 10
    • 0034834616 scopus 로고    scopus 로고
    • Individual interactions influence the crystalline order for membrane proteins
    • Camara-Artigas A, Magee CL, Williams JC and Allen JP (2001) Individual interactions influence the crystalline order for membrane proteins. Acta Crystallogr D 57: 1281-1286
    • (2001) Acta Crystallogr D , vol.57 , pp. 1281-1286
    • Camara-Artigas, A.1    Magee, C.L.2    Williams, J.C.3    Allen, J.P.4
  • 11
    • 0037143641 scopus 로고    scopus 로고
    • Interactions between lipids and bacterial reaction centers determined by protein crystallography
    • Camara-Artigas A, Brune D and Allen JP (2002a) Interactions between lipids and bacterial reaction centers determined by protein crystallography. Proc Natl Acad Sci USA 99: 11055-11060
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11055-11060
    • Camara-Artigas, A.1    Brune, D.2    Allen, J.P.3
  • 12
    • 0036440896 scopus 로고    scopus 로고
    • The structure of the heterodimer reaction center from Rhodobacter sphaeroides at 2.55 Å resolution
    • Camara-Artigas A, Magee C, Goetsch A and Allen JP (2002b) The structure of the heterodimer reaction center from Rhodobacter sphaeroides at 2.55 Å resolution. Photosynth Res 74: 87-93
    • (2002) Photosynth Res , vol.74 , pp. 87-93
    • Camara-Artigas, A.1    Magee, C.2    Goetsch, A.3    Allen, J.P.4
  • 13
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50: 760-763
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 14
    • 0025784505 scopus 로고
    • The structure of the membrane-bound photosynthetic reaction center from Rhodobacter sphaeroides
    • Chang CH, El-Kabbani O, Tiede DM, Norris JR and Schiffer M (1991) The structure of the membrane-bound photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry 30: 5352-5360
    • (1991) Biochemistry , vol.30 , pp. 5352-5360
    • Chang, C.H.1    El-Kabbani, O.2    Tiede, D.M.3    Norris, J.R.4    Schiffer, M.5
  • 15
    • 0028281478 scopus 로고
    • Crystallographic analyses of site-directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides
    • Chirino AJ, Lous EJ, Huber M, Allen JP, Schenck CC, Paddock ML, Feher G and Rees DC (1994) Crystallographic analyses of site-directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry 33: 4584-4593
    • (1994) Biochemistry , vol.33 , pp. 4584-4593
    • Chirino, A.J.1    Lous, E.J.2    Huber, M.3    Allen, J.P.4    Schenck, C.C.5    Paddock, M.L.6    Feher, G.7    Rees, D.C.8
  • 16
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution
    • Deisenhofer J, Epp O, Miki K, Huber R and Michel H (1985) Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution. Nature 318: 618-624
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 17
    • 0028957690 scopus 로고
    • Crystallographic refinement at 2.3 Å resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis
    • Deisenhofer J, Epp O, Sinning I and Michel H (1995) Crystallographic refinement at 2.3 Å resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis. J Mol Biol 246: 429-457
    • (1995) J Mol Biol , vol.246 , pp. 429-457
    • Deisenhofer, J.1    Epp, O.2    Sinning, I.3    Michel, H.4
  • 18
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh RA and Huber R (1991) Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr A 47: 392-400
    • (1991) Acta Crystallogr a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 19
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions
    • Ermler U, Fritzsch G, Buchanan SK and Michel H (1994) Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: cofactors and protein-cofactor interactions. Structure 2: 925-936
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 20
    • 0031751696 scopus 로고    scopus 로고
    • Crystallization of bacterial reaction centers
    • Fritzsch G (1998) Crystallization of bacterial reaction centers. Methods Enzymol 297: 57-77
    • (1998) Methods Enzymol , vol.297 , pp. 57-77
    • Fritzsch, G.1
  • 21
    • 0036795645 scopus 로고    scopus 로고
    • Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria
    • Fritzsch G, Koepke J, Diem R, Kuglstatter A and Baciou L (2002) Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria. Acta Crystallogr D58: 1660-1663
    • (2002) Acta Crystallogr D , vol.58 , pp. 1660-1663
    • Fritzsch, G.1    Koepke, J.2    Diem, R.3    Kuglstatter, A.4    Baciou, L.5
  • 23
    • 0034705174 scopus 로고    scopus 로고
    • Structural consequences of the replacement of glycine M203 with aspartic acid in the reaction center from Rhodobacter sphaeroides
    • Fyfe PK, Ridge JP, McAuley KE, Cogdell RJ, Isaacs NW and Jones MR (2000) Structural consequences of the replacement of glycine M203 with aspartic acid in the reaction center from Rhodobacter sphaeroides. Biochemistry 39: 5953-5960
    • (2000) Biochemistry , vol.39 , pp. 5953-5960
    • Fyfe, P.K.1    Ridge, J.P.2    McAuley, K.E.3    Cogdell, R.J.4    Isaacs, N.W.5    Jones, M.R.6
  • 25
    • 84893482610 scopus 로고
    • Solution for best rotation to relate 2 sets of vectors
    • Kabsch W (1976) Solution for best rotation to relate 2 sets of vectors. Acta Crystallogr A 32: 922-923
    • (1976) Acta Crystallogr A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 26
    • 0043095535 scopus 로고    scopus 로고
    • Lipidic cubic phase crystal structure of the photosynthetic reaction center from Rhodobacter sphaeroides at 2.35 Å resolution
    • Katona G, Andreasson U, Landau EM, Andreasson LE and Neutze R (2003) Lipidic cubic phase crystal structure of the photosynthetic reaction center from Rhodobacter sphaeroides at 2.35 Å resolution. J Mol Biol 331: 681-692
    • (2003) J Mol Biol , vol.331 , pp. 681-692
    • Katona, G.1    Andreasson, U.2    Landau, E.M.3    Andreasson, L.E.4    Neutze, R.5
  • 27
    • 0030589514 scopus 로고    scopus 로고
    • Phi/psi-chology: Ramachandran revisited
    • Kleywegt GJ and Jones TA (1996) Phi/psi-chology: Ramachandran revisited. Structure 4: 1395-1400
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 28
    • 0035836485 scopus 로고    scopus 로고
    • X-ray structure analyses of photosynthetic reaction center variants from Rhodobacter sphaeroides: Structural changes induced by point mutations at position L209 modulate electron and proton transfer
    • Kuglstatter A, Ermler U, Michel H, Baciou L and Fritzsch G (2001) X-ray structure analyses of photosynthetic reaction center variants from Rhodobacter sphaeroides: structural changes induced by point mutations at position L209 modulate electron and proton transfer. Biochemistry 40: 4253-4260
    • (2001) Biochemistry , vol.40 , pp. 4253-4260
    • Kuglstatter, A.1    Ermler, U.2    Michel, H.3    Baciou, L.4    Fritzsch, G.5
  • 30
    • 0032877515 scopus 로고    scopus 로고
    • Quinone-binding sites in membrane proteins: What can we learn from the Rhodopseudomonas viridis reaction center?
    • Lancaster CR (1999) Quinone-binding sites in membrane proteins: what can we learn from the Rhodopseudomonas viridis reaction center? Biochem Soc Trans 27: 591-596
    • (1999) Biochem Soc Trans , vol.27 , pp. 591-596
    • Lancaster, C.R.1
  • 31
    • 0033605220 scopus 로고    scopus 로고
    • Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid
    • Lancaster CR and Michel H (1999) Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid. J Mol Biol 286: 883-898
    • (1999) J Mol Biol , vol.286 , pp. 883-898
    • Lancaster, C.R.1    Michel, H.2
  • 32
    • 0034671487 scopus 로고    scopus 로고
    • Structural basis of the drastically increased initial electron transfer rate in the reaction renter from a Rhodopseudomonas viridis mutant described at 2.00-Å resolution
    • Lancaster CRD, Bibikova MV, Sabatino P, Oesterhelt D and Michel H (2000) Structural basis of the drastically increased initial electron transfer rate in the reaction renter from a Rhodopseudomonas viridis mutant described at 2.00-Å resolution. J Biol Chem 275: 39364-39368
    • (2000) J Biol Chem , vol.275 , pp. 39364-39368
    • Lancaster, C.R.D.1    Bibikova, M.V.2    Sabatino, P.3    Oesterhelt, D.4    Michel, H.5
  • 33
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS and Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26: 283-291
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 34
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee AG (2003) Lipid-protein interactions in biological membranes: a structural perspective. Biochim Biophys Acta 1612: 1-40
    • (2003) Biochim Biophys Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 35
    • 0031583476 scopus 로고    scopus 로고
    • Crystal structure of the bacteriochlorophyll a protein from Chlorobium tepidum
    • Li YF, Zhou WL, Blankenship RE and Allen JP (1997) Crystal structure of the bacteriochlorophyll a protein from Chlorobium tepidum. J Mol Biol 271: 456-471
    • (1997) J Mol Biol , vol.271 , pp. 456-471
    • Li, Y.F.1    Zhou, W.L.2    Blankenship, R.E.3    Allen, J.P.4
  • 36
    • 0032492681 scopus 로고    scopus 로고
    • Structural studies of wild type and mutant reaction centres from an antenna-deficient strain of Rhodobacter sphaeroides: Monitoring the optical properties of the complex from bacterial cell to crystal
    • McAuley-Hecht K, Fyfe P, Ridge JP, Prince S, Hunter CN, Isaacs NW, Cogdell RJ and Jones MR (1998) Structural studies of wild type and mutant reaction centres from an antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical properties of the complex from bacterial cell to crystal. Biochemistry 37: 4740-4750
    • (1998) Biochemistry , vol.37 , pp. 4740-4750
    • McAuley-Hecht, K.1    Fyfe, P.2    Ridge, J.P.3    Prince, S.4    Hunter, C.N.5    Isaacs, N.W.6    Cogdell, R.J.7    Jones, M.R.8
  • 38
    • 0020475570 scopus 로고
    • Three-dimensional crystals of a membrane protein complex: The photosynthetic reaction centre from Rhodopseudomonas viridis
    • Michel H (1982) Three-dimensional crystals of a membrane protein complex: the photosynthetic reaction centre from Rhodopseudomonas viridis. J Mol Biol 158: 567-572
    • (1982) J Mol Biol , vol.158 , pp. 567-572
    • Michel, H.1
  • 40
    • 0034610266 scopus 로고    scopus 로고
    • Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: Thermostability and electron transfer
    • Nogi T, Fathir I, Kobayashi M, Nozawa T and Miki K (2000) Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer. Proc Natl Acad Sci USA 97: 13561-13566
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13561-13566
    • Nogi, T.1    Fathir, I.2    Kobayashi, M.3    Nozawa, T.4    Miki, K.5
  • 41
    • 0037076542 scopus 로고    scopus 로고
    • The structure of a mutant photosynthetic reaction center shows unexpected changes in main chain orientations and quinone position
    • Pokkuluri PR, Laible PD, Deng YL, Wong TN, Hanson DK and Schiffer M (2002) The structure of a mutant photosynthetic reaction center shows unexpected changes in main chain orientations and quinone position. Biochemistry 41: 5998-6007
    • (2002) Biochemistry , vol.41 , pp. 5998-6007
    • Pokkuluri, P.R.1    Laible, P.D.2    Deng, Y.L.3    Wong, T.N.4    Hanson, D.K.5    Schiffer, M.6
  • 42
    • 0030598343 scopus 로고    scopus 로고
    • Deviations from standard atomic volumes as a quality measure for protein crystal structures
    • Pontius J, Richelle J and Wodak SJ (1996) Deviations from standard atomic volumes as a quality measure for protein crystal structures. J Mol Biol 264: 121-136
    • (1996) J Mol Biol , vol.264 , pp. 121-136
    • Pontius, J.1    Richelle, J.2    Wodak, S.J.3
  • 44
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron and proton transfer
    • Stowell MHB, McPhillips TM, Rees DC, Soltis SM, Abresch E and Feher G (1997) Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron and proton transfer. Science 276: 812-816
    • (1997) Science , vol.276 , pp. 812-816
    • Stowell, M.H.B.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 45
    • 0036075164 scopus 로고    scopus 로고
    • Life science applications of the Cambridge structural database
    • Taylor R (2002) Life science applications of the Cambridge structural database. Acta Crystallogr D 58: 879-888
    • (2002) Acta Crystallogr D , vol.58 , pp. 879-888
    • Taylor, R.1
  • 46
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modelling and drug design program
    • Vriend G (1990) WHAT IF: a molecular modelling and drug design program. J Mol Graphics 8: 52-56
    • (1990) J Mol Graphics , vol.8 , pp. 52-56
    • Vriend, G.1


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