메뉴 건너뛰기




Volumn 508, Issue 7495, 2014, Pages 228-232

Structure of the LH1-RC complex from Thermochromatium tepidum at 3.0 Å

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOCHLOROPHYLL; HETERODIMER; UBIQUINONE; CALCIUM; RHODOVIOLASCIN; XANTHOPHYLL;

EID: 84900331836     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13197     Document Type: Article
Times cited : (194)

References (46)
  • 1
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3A° resolution
    • Deisenhofer, J., Epp, O., Miki, K., Huber, R. & Michel, H. Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3A° resolution. Nature 318, 618-624 (1985).
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 2
    • 0023408258 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The protein subunits
    • Allen, J. P., Feher, G., Yeates, T. O., Komiya, H. & Rees, D. C. Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits. Proc. Natl Acad. Sci. USA 84, 6162-6166 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 6162-6166
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 3
    • 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. & Miki, K. 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).
    • (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
  • 4
    • 0029637583 scopus 로고
    • Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria
    • McDermott, G. et al. Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria. Nature 374, 517-521 (1995).
    • (1995) Nature , vol.374 , pp. 517-521
    • McDermott, G.1
  • 5
    • 0030585121 scopus 로고    scopus 로고
    • The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum
    • Koepke, J., Hu, X., Muenke, C., Schulten, K. & Michel, H. The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum. Structure 4, 581-597 (1996).
    • (1996) Structure , vol.4 , pp. 581-597
    • Koepke, J.1    Hu, X.2    Muenke, C.3    Schulten, K.4    Michel, H.5
  • 6
    • 0035979355 scopus 로고    scopus 로고
    • 3 light-harvesting complex from the purple bacteria Rhodopseudomonas acidophila strain 7050
    • 3 light-harvesting complex from the purple bacteria Rhodopseudomonas acidophila strain 7050. Biochemistry 40, 8783-8789 (2001).
    • (2001) Biochemistry , vol.40 , pp. 8783-8789
    • McLuskey, K.1    Prince, S.M.2    Cogdell, R.J.3    Isaacs, N.W.4
  • 7
    • 0028953308 scopus 로고
    • The 8.5A° projection map of the lightharvesting complex i from Rhodospirillum rubrum reveals a ring composed of 16 subunits
    • Karrasch, S., Bullough, P. A. & Ghosh, R. The 8.5A° projection map of the lightharvesting complex I from Rhodospirillum rubrum reveals a ring composed of 16 subunits. EMBO J. 14, 631-638 (1995).
    • (1995) EMBO J. , vol.14 , pp. 631-638
    • Karrasch, S.1    Bullough, P.A.2    Ghosh, R.3
  • 8
    • 0036683068 scopus 로고    scopus 로고
    • Projection structure of the photosynthetic reaction centre-antenna complex of Rhodospirillum rubrumat 8.5A° resolution
    • Jamieson, S. J. et al. Projection structure of the photosynthetic reaction centre-antenna complex of Rhodospirillum rubrumat 8.5A° resolution. EMBO J. 21, 3927-3935 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3927-3935
    • Jamieson, S.J.1
  • 9
    • 0037452675 scopus 로고    scopus 로고
    • Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core complex in native membranes by AFM
    • Scheuring, S. et al. Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core complex in native membranes by AFM. Proc. Natl Acad. Sci. USA 100, 1690-1693 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1690-1693
    • Scheuring, S.1
  • 10
    • 0942287196 scopus 로고    scopus 로고
    • Structural role of PufX in the dimerization of the photosynthetic core complex of Rhodobacter sphaeroides
    • Scheuring, S. et al. Structural role of PufX in the dimerization of the photosynthetic core complex of Rhodobacter sphaeroides. J. Biol. Chem. 279, 3620-3626 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 3620-3626
    • Scheuring, S.1
  • 11
    • 0033081638 scopus 로고    scopus 로고
    • Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides
    • Jungas, C., Ranck, J. L., Rigaud, J. L., Joliot, P. & Verméglio, A. Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides.EMBO J. 18, 534-542 (1999).
    • (1999) EMBO J , vol.18 , pp. 534-542
    • Jungas, C.1    Ranck, J.L.2    Rigaud, J.L.3    Joliot, P.4    Verméglio, A.5
  • 12
    • 1842510034 scopus 로고    scopus 로고
    • Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: The role of PufX
    • Siebert, C. A. et al. Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: the role of PufX. EMBO J. 23, 690-700 (2004).
    • (2004) EMBO J. , vol.23 , pp. 690-700
    • Siebert, C.A.1
  • 13
    • 20344374627 scopus 로고    scopus 로고
    • The 8.5A° projection structure of the core RC-LH1-PufX dimer ofRhodobacter sphaeroides
    • Qian, P., Hunter, C. N. & Bullough, P. A. The 8.5A° projection structure of the core RC-LH1-PufX dimer ofRhodobacter sphaeroides. J.Mol. Biol. 349,948-960(2005).
    • (2005) J.Mol. Biol. , vol.349 , pp. 948-960
    • Qian, P.1    Hunter, C.N.2    Bullough, P.A.3
  • 14
    • 12544254339 scopus 로고    scopus 로고
    • Structure of the dimeric PufX-containing core complex of Rhodobacter blasticus by in situ atomic force microscopy
    • Scheuring, S., Busselez, J. & Lévy, D. Structure of the dimeric PufX-containing core complex of Rhodobacter blasticus by in situ atomic force microscopy. J. Biol. Chem. 280, 1426-1431 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 1426-1431
    • Scheuring, S.1    Busselez, J.2    Lévy, D.3
  • 15
    • 0346874216 scopus 로고    scopus 로고
    • Crystal structure of the RC-LH1 core complex from Rhodopseudomonas palustris
    • Roszak, A. W. et al. Crystal structure of the RC-LH1 core complex from Rhodopseudomonas palustris. Science 302, 1969-1972 (2003).
    • (2003) Science , vol.302 , pp. 1969-1972
    • Roszak, A.W.1
  • 16
    • 38049146157 scopus 로고    scopus 로고
    • Refinement of the X-ray structure of the RC-LH1 core complex from Rhodopseudomonas palustris by single-molecule spectroscopy
    • Richter, M. F. et al. Refinement of the X-ray structure of the RC-LH1 core complex from Rhodopseudomonas palustris by single-molecule spectroscopy. Proc. Natl Acad. Sci. USA 104, 20280-20284 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 20280-20284
    • Richter, M.F.1
  • 17
    • 34547131088 scopus 로고    scopus 로고
    • Purification, characterization and crystallization of the core complex from thermophilic purple sulfur bacteriumThermochromatium tepidum
    • Suzuki, H. et al. Purification, characterization and crystallization of the core complex from thermophilic purple sulfur bacteriumThermochromatium tepidum. Biochim. Biophys. Acta 1767, 1057-1063 (2007).
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1057-1063
    • Suzuki, H.1
  • 18
    • 0001054397 scopus 로고
    • A novel photosynthetic purple bacterium isolated from a Yellowstone hot spring
    • Madigan, M. T. A novel photosynthetic purple bacterium isolated from a Yellowstone hot spring. Science 225, 313-315 (1984).
    • (1984) Science , vol.225 , pp. 313-315
    • Madigan, M.T.1
  • 20
    • 46649111231 scopus 로고    scopus 로고
    • Calcium ions are involved in the unusual red shift of the light-harvesting 1 Qy transition of the core complex in thermophilic purple sulfur bacteriumThermochromatiumtepidum
    • Kimura, Y. et al. Calcium ions are involved in the unusual red shift of the light-harvesting 1 Qy transition of the core complex in thermophilic purple sulfur bacteriumThermochromatiumtepidum. J. Biol. Chem. 283, 13867-13873 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 13867-13873
    • Kimura, Y.1
  • 21
    • 58649102492 scopus 로고    scopus 로고
    • Calciumions are required for the enhanced thermal stability of the light-harvesting-reaction center core complex from thermophilic purple sulfur bacteriumThermochromatium tepidum
    • Kimura, Y., Yu, L. J., Hirano, Y., Suzuki, H.&Wang, Z.-Y. Calciumions are required for the enhanced thermal stability of the light-harvesting-reaction center core complex from thermophilic purple sulfur bacteriumThermochromatium tepidum. J. Biol. Chem. 284, 93-99 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 93-99
    • Kimura, Y.1    Yu, L.J.2    Hirano, Y.3    Suzuki, H.4    Wang, Z.-Y.5
  • 22
    • 78650872632 scopus 로고    scopus 로고
    • Examination of the putative Ca21-binding site in the light-harvesting complex 1 of thermophilic purple sulfur bacterium Thermochromatium tepidum
    • Yu, L. J., Kato, S. & Wang, Z.-Y. Examination of the putative Ca21-binding site in the light-harvesting complex 1 of thermophilic purple sulfur bacterium Thermochromatium tepidum. Photosynth. Res. 106, 215-220 (2010).
    • (2010) Photosynth. Res. , vol.106 , pp. 215-220
    • Yu, L.J.1    Kato, S.2    Wang, Z.-Y.3
  • 23
    • 0037424652 scopus 로고    scopus 로고
    • 2 complex from Rps. Acidophila at 2.0A° resolution and 100K: New structural features and functionally relevant motions
    • 2 complex from Rps. acidophila at 2.0A° resolution and 100K: new structural features and functionally relevant motions. J. Mol. Biol. 326, 1523-1538 (2003).
    • (2003) J. Mol. Biol. , vol.326 , pp. 1523-1538
    • Papiz, M.Z.1    Prince, S.M.2    Howard, T.3    Cogdell, R.J.4    Isaacs, N.W.5
  • 24
    • 0032437780 scopus 로고    scopus 로고
    • Biochemicalandspectral characterizationof the core light harvesting complex 1 (LH1) from the thermophilic purple sulfur bacterium Chromatium tepidum
    • Fathir, I. et al. Biochemicalandspectral characterizationof the core light harvesting complex 1 (LH1) from the thermophilic purple sulfur bacterium Chromatium tepidum. Photosynth. Res. 58, 193-202 (1998).
    • (1998) Photosynth. Res. , vol.58 , pp. 193-202
    • Fathir, I.1
  • 25
    • 84860803265 scopus 로고    scopus 로고
    • Metal cations modulate the bacteriochlorophyll-protein interaction in the light-harvesting 1 core complex from Thermochromatium tepidum
    • Kimura, Y. et al. Metal cations modulate the bacteriochlorophyll-protein interaction in the light-harvesting 1 core complex from Thermochromatium tepidum. Biochim. Biophys. Acta 1817, 1022-1029 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1022-1029
    • Kimura, Y.1
  • 26
    • 0028927242 scopus 로고
    • Reconstitution of the bacterial core light-harvesting complexes of Rhodobacter sphaeroides andRhodospirillumrubrum with isolated a-and b-polypeptides, bacteriochlorophyll a, and carotenoid
    • Davis, C. M., Bustamante, P. L. & Loach, P. A. Reconstitution of the bacterial core light-harvesting complexes of Rhodobacter sphaeroides andRhodospirillumrubrum with isolated a-and b-polypeptides, bacteriochlorophyll a, and carotenoid. J. Biol. Chem. 270, 5793-5804 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 5793-5804
    • Davis, C.M.1    Bustamante, P.L.2    Loach, P.A.3
  • 27
    • 0031575413 scopus 로고    scopus 로고
    • Two-dimensional crystallization of the light-harvesting I-reaction centre photounit fromRhodospirillumrubrum
    • Walz, T. & Ghosh, R. Two-dimensional crystallization of the light-harvesting I-reaction centre photounit fromRhodospirillumrubrum. J. Mol. Biol. 265, 107-111 (1997).
    • (1997) J. Mol. Biol. , vol.265 , pp. 107-111
    • Walz, T.1    Ghosh, R.2
  • 28
    • 2442667942 scopus 로고    scopus 로고
    • Flexibility and size heterogeneity of the LH1 light harvesting complex revealed by atomic force microscopy
    • Bahatyrova, S. et al. Flexibility and size heterogeneity of the LH1 light harvesting complex revealed by atomic force microscopy. J. Biol. Chem. 279, 21327-21333 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 21327-21333
    • Bahatyrova, S.1
  • 29
    • 84912130176 scopus 로고    scopus 로고
    • eds Hunter, C. N., Daldal, F. & Beatty, J. T.) Springer
    • Scheuring, S. in The purple phototrophic bacteria (eds Hunter, C. N., Daldal, F. & Beatty, J. T.) 941-952 (Springer, 2009).
    • (2009) The Purple Phototrophic Bacteria , pp. 941-952
    • Scheuring, S.1
  • 30
    • 15744405284 scopus 로고    scopus 로고
    • Functional consequences of the organization of the photosynthetic apparatus in Rhodobacter sphaeroides: II. A study of PufX-membranes
    • Comayras, F., Jungas, C. & Lavergne, J. Functional consequences of the organization of the photosynthetic apparatus in Rhodobacter sphaeroides: II. A study of PufX-membranes. J. Biol. Chem. 280, 11214-11223 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 11214-11223
    • Comayras, F.1    Jungas, C.2    Lavergne, J.3
  • 31
    • 56749177094 scopus 로고    scopus 로고
    • Organisation and function of the Phaeospirillum molischianum photosynthetic apparatus
    • Mascle-Allemand, C., Lavergne, J., Bernadac, A. & Sturgis, J. N. Organisation and function of the Phaeospirillum molischianum photosynthetic apparatus. Biochim. Biophys. Acta 1777, 1552-1559 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1552-1559
    • Mascle-Allemand, C.1    Lavergne, J.2    Bernadac, A.3    Sturgis, J.N.4
  • 32
    • 33846008719 scopus 로고    scopus 로고
    • Possible pathway for ubiquinone shuttling in Rhodospirillum rubrum revealed by molecular dynamics simulation
    • Aird, A., Wrachtrup, J., Schulten, K. & Tietz, C. Possible pathway for ubiquinone shuttling in Rhodospirillum rubrum revealed by molecular dynamics simulation. Biophys. J. 92, 23-33 (2007).
    • (2007) Biophys. J. , vol.92 , pp. 23-33
    • Aird, A.1    Wrachtrup, J.2    Schulten, K.3    Tietz, C.4
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A. & Teplyakov, A. MOLREP: an automated program for molecular replacement. J. Appl. Cryst. 30, 1022-1025 (1997).
    • (1997) J. Appl. Cryst. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 35
    • 0028103275 scopus 로고
    • The CCP4suite: Programs for protein crystallography
    • Number 4
    • Collaborative Computational Project, Number 4. The CCP4suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
    • Collaborative Computational Project1
  • 36
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution, density modification, and model building
    • Terwilliger, T. SOLVE and RESOLVE: automated structure solution, density modification, and model building. J. Synchrotron Radiat. 11, 49-52 (2004).
    • (2004) J. Synchrotron Radiat. , vol.11 , pp. 49-52
    • Terwilliger, T.1
  • 37
    • 0002583957 scopus 로고
    • 'Dm': An automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newsl
    • Cowtan, K. 'dm': An automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newsl. Prot. Crystallogr. 31, 34-38 (1994).
    • (1994) Prot. Crystallogr. , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 38
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125, 156-165 (1999).
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 40
    • 80052470285 scopus 로고    scopus 로고
    • Automated real-space refinement of protein structure using a realistic backbone move set
    • Haddadian, E. J. et al. Automated real-space refinement of protein structure using a realistic backbone move set. Biophys. J. 101, 899-909 (2011).
    • (2011) Biophys. J. , vol.101 , pp. 899-909
    • Haddadian, E.J.1
  • 41
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 42
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 43
    • 0000243829 scopus 로고
    • PROCHECK - A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK - a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291 (1993).
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 45
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features
    • Kabsch, W. & Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 46
    • 0030822870 scopus 로고    scopus 로고
    • The genes coding for the L, M and cytochrome subunits of the photosynthetic reaction center from the thermophilic purple sulfur bacterium Chromatium tepidum
    • Fathir, I. et al. The genes coding for the L, M and cytochrome subunits of the photosynthetic reaction center from the thermophilic purple sulfur bacterium Chromatium tepidum. Photosynth. Res. 51, 71-82 (1997).
    • (1997) Photosynth. Res. , vol.51 , pp. 71-82
    • Fathir, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.