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Volumn 141, Issue 2, 2003, Pages 149-155

The 1.45 Å three-dimensional structure of C-phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus

Author keywords

3D structure; Crystallization; Light harvesting antenna; Photosynthesis; Soluble extrinsic hexameric complex; X ray crystallography

Indexed keywords

C PHYCOCYANIN; PHYCOBILIPROTEIN; PHYCOCYANIN; UNCLASSIFIED DRUG;

EID: 0037291310     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1047-8477(02)00609-3     Document Type: Article
Times cited : (65)

References (25)
  • 1
    • 0035850751 scopus 로고    scopus 로고
    • Structure of c-phycocyanin from the thermophilic cyanobacterium Synechococcus vulcanus at 2.5 Å: Structural implications for thermal stability in phycobilisome assembly
    • Adir N., Dobrovetsky Y., Lerner N. Structure of c-phycocyanin from the thermophilic cyanobacterium Synechococcus vulcanus at 2.5. Å: structural implications for thermal stability in phycobilisome assembly J. Mol. Biol. 313:2001;71-81.
    • (2001) J. Mol. Biol. , vol.313 , pp. 71-81
    • Adir, N.1    Dobrovetsky, Y.2    Lerner, N.3
  • 2
    • 0026597444 scopus 로고
    • Free R-value - A novel statistical quantity for assessing the accuracy of crystal-structures
    • Brunger A.T. Free R-value - A novel statistical quantity for assessing the accuracy of crystal-structures. Nature. 355:1992;472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 3
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. A 50, 760-763.
    • (1994) Acta Crystallogr. Sect. A , vol.50 , pp. 760-763
  • 4
    • 0002663405 scopus 로고    scopus 로고
    • Protein Precision Re-examined: Luzzati Plots Do Not Estimate Final Errors
    • Daresbury Laboratory, Warrington, UK
    • Cruickshank, D.W.J., 1996. Protein Precision Re-examined: Luzzati Plots Do Not Estimate Final Errors. In: Proceedings of the CCP4 Study Weekend, Daresbury Laboratory, Warrington, UK.
    • (1996) Proceedings of the CCP4 Study Weekend
    • Cruickshank, D.W.J.1
  • 5
    • 0029305364 scopus 로고
    • Comparison of calculated and experimentally resolved rate constants for excitation energy transfer in C-phycocyanin. 2. Trimers
    • Debreczeny M.P., Sauer K.H., Zhou J., Bryant D.A. Comparison of calculated and experimentally resolved rate constants for excitation energy transfer in C-phycocyanin. 2. Trimers. J. Phys. Chem. 99:1995;8420-8431.
    • (1995) J. Phys. Chem. , vol.99 , pp. 8420-8431
    • Debreczeny, M.P.1    Sauer, K.H.2    Zhou, J.3    Bryant, D.A.4
  • 6
    • 0344863070 scopus 로고    scopus 로고
    • Reconstitution, characterisation and mass analysis of the pentacylindrical allophycocyanin core complex from the cyanobacterium Anabaena sp. PCC 7120
    • Ducret A., Muller S.A., Goldie K.N., Hefti A., Sidler W.A., Zuber H., Engel A. Reconstitution, characterisation and mass analysis of the pentacylindrical allophycocyanin core complex from the cyanobacterium Anabaena sp. PCC 7120. J. Mol. Biol. 278:1998;369-388.
    • (1998) J. Mol. Biol. , vol.278 , pp. 369-388
    • Ducret, A.1    Muller, S.A.2    Goldie, K.N.3    Hefti, A.4    Sidler, W.A.5    Zuber, H.6    Engel, A.7
  • 7
    • 0025967561 scopus 로고
    • Isolation, crystallization, crystal structure analysis and refinement of constitutive C-phycocyanin from the chromatically adapting cyanobacterium Fremyella diplosiphon at 1.66 Å resolution
    • Duerring M., Schmidt G.B., Huber R. Isolation, crystallization, crystal structure analysis and refinement of constitutive C-phycocyanin from the chromatically adapting cyanobacterium Fremyella diplosiphon at 1.66. Å resolution J. Mol. Biol. 217:1991;577-592.
    • (1991) J. Mol. Biol. , vol.217 , pp. 577-592
    • Duerring, M.1    Schmidt, G.B.2    Huber, R.3
  • 8
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein-structure refinement
    • Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein-structure refinement. Acta Crystallogr. Sect. A. 47:1991;392-400.
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 10
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., Krauss N. Three-dimensional structure of cyanobacterial photosystem I at 2.5. Å resolution Nature. 411:2001;909-917.
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 11
    • 0029911269 scopus 로고    scopus 로고
    • Photosystem I at 4 Å resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system
    • Krauss N., Schubert W.D., Klukas O., Fromme P., Witt H.T., Saenger W. Photosystem I at 4. Å resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system Nature Struct. Biol. 3:1996;965-973.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 965-973
    • Krauss, N.1    Schubert, W.D.2    Klukas, O.3    Fromme, P.4    Witt, H.T.5    Saenger, W.6
  • 13
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D. 53:1997;240-255.
    • (1997) Acta Crystallogr. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 14
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. Sect. A. 50:1994;157-163.
    • (1994) Acta Crystallogr. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 15
    • 0034623285 scopus 로고    scopus 로고
    • Three-dimensional structure of Chlamydomonas reinhardtii and Synechococcus elongatus photosystem II complexes allows for comparison of their oxygen-evolving complex organization
    • Nield J., Kruse O., Ruprecht J., da Fonseca P., Buchel C., Barber J. Three-dimensional structure of Chlamydomonas reinhardtii and Synechococcus elongatus photosystem II complexes allows for comparison of their oxygen-evolving complex organization. J. Biol. Chem. 275:2000;27940-27946.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27940-27946
    • Nield, J.1    Kruse, O.2    Ruprecht, J.3    Da Fonseca, P.4    Buchel, C.5    Barber, J.6
  • 17
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read R.J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. Sect. A. 42:1986;140-149.
    • (1986) Acta Crystallogr. Sect. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 18
    • 0029670313 scopus 로고    scopus 로고
    • How does photosystem 2 split water? The structural basis of efficient energy conservation
    • Rögner M., Boekema E.J., Barber J. How does photosystem 2 split water? The structural basis of efficient energy conservation. Trends Biochem. Sci. 21:1996;44-49.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 44-49
    • Rögner, M.1    Boekema, E.J.2    Barber, J.3
  • 19
    • 0037304614 scopus 로고    scopus 로고
    • Systematic improvement of protein crystals by determining the supersolubility curves of phase diagrams
    • in press
    • Saridakis, E., Chayen, N.E., 2003. Systematic improvement of protein crystals by determining the supersolubility curves of phase diagrams. Biophys. J., in press.
    • (2003) Biophys. J.
    • Saridakis, E.1    Chayen, N.E.2
  • 20
    • 0023645201 scopus 로고
    • Refined three-dimensional structures of two cyanobacterial C-phycocyanins at 2.1 and 2.5 Å resolution. A common principle of phycobilin-protein interaction
    • Schirmer T., Bode W., Huber R. Refined three-dimensional structures of two cyanobacterial C-phycocyanins at 2.1 and 2.5. Å resolution. A common principle of phycobilin-protein interaction J. Mol. Biol. 196:1987;677-695.
    • (1987) J. Mol. Biol. , vol.196 , pp. 677-695
    • Schirmer, T.1    Bode, W.2    Huber, R.3
  • 21
  • 22
    • 0033047094 scopus 로고    scopus 로고
    • Crystal structure of C-phycocyanin from Cyanidium caldarium provides a new perspective on phycobilisome assembly
    • Stec B., Troxler R.F., Teeter M.M. Crystal structure of C-phycocyanin from Cyanidium caldarium provides a new perspective on phycobilisome assembly. Biophys. J. 76:1999;2912-2921.
    • (1999) Biophys. J. , vol.76 , pp. 2912-2921
    • Stec, B.1    Troxler, R.F.2    Teeter, M.M.3
  • 23
    • 0034819768 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of the light-harvesting protein phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus
    • Toriumi Y., Park S.Y., Hashimoto H., Shimizu H., Hirano M., Kamiya N. Crystallization and preliminary X-ray diffraction analysis of the light-harvesting protein phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus. Acta Crystallogr. Sect. D. 57:2001;1326-1328.
    • (2001) Acta Crystallogr. Sect. D , vol.57 , pp. 1326-1328
    • Toriumi, Y.1    Park, S.Y.2    Hashimoto, H.3    Shimizu, H.4    Hirano, M.5    Kamiya, N.6
  • 24
    • 0034989667 scopus 로고    scopus 로고
    • Structure of C-phycocyanin from Spirulina platensis at 2.2 Å resolution: A novel monoclinic crystal form for phycobiliproteins in phycobilisomes
    • Wang X.Q., Li L.N., Chang W.R., Zhang J.P., Gui L.L., Guo B.J., Liang D.C. Structure of C-phycocyanin from Spirulina platensis at 2.2. Å resolution: a novel monoclinic crystal form for phycobiliproteins in phycobilisomes Acta Crystallogr. Sect. D. 57:2001;784-792.
    • (2001) Acta Crystallogr. Sect. D , vol.57 , pp. 784-792
    • Wang, X.Q.1    Li, L.N.2    Chang, W.R.3    Zhang, J.P.4    Gui, L.L.5    Guo, B.J.6    Liang, D.C.7
  • 25
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Ångstrom resolution
    • Zouni A., Witt H.T., Kern J., Fromme P., Krauss N., Saenger W., Orth P. Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Ångstrom 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.