Solution structure of cytochrome c6 from the thermophilic cyanobacterium Synechococcus elongatus

EMBO Journal

Volumn 17, Issue 1, 1998, Pages 27-36

  Beißinger, Martina ^b   Sticht, Heinrich ^b   Sutter, Martin ^a,b   Ejchart, Andrzej ^b   Haehnel, Wolfgang ^a,b   Rösch, Paul ^b  

^a UNIVERSITY OF FREIBURG   (Germany)

^b UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

Cytochrome c6; Electron transport; Photosynthesis; Protein conformation; Synechococcus elongatus

Indexed keywords

CYTOCHROME C; CYTOCHROME F;

ARTICLE; CYANOBACTERIUM; ELECTRON TRANSPORT; EVOLUTION; GRAM NEGATIVE BACTERIUM; MOLECULAR DYNAMICS; MUTAGENESIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; CYANOBACTERIA; CYTOCHROMES; CYTOCHROMES F; ELECTRON TRANSPORT; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SOLUTIONS;

EID: 0012043156     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.1.27     Document Type: Article

References (53)

1. Banci, L., Bertini, I., Quacquarini, G., Walter, O., Diaz, A., Hervás, M. and De la Rosa, M.A. (1996) The solution structure of cytochrome c6 from the green alga M.braunii. J. Biol. Inorg. Chem. 1, 330-340.
2. 2] ferredoxin in solution. Biochemistry, 35, 12831-12841.
3. 13C enriched proteins. J. Biomol. NMR, 1, 99-104.
4. Bax, A., Griffey, R.H. and Hawkins, B.L. (1983) Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR. J. Magn. Resonance, 55, 301-312.
5. Berendsen, H.J.C., Postma, J.P.M., van Gunsteren, W.F., DiNiola, A. and Haak, J.R. (1984) Molecular dynamics with coupling to an external bath. J. Chem. Phys., 81, 3684-3690.
6. Brünger, A.T. (1993) X-PLOR Version 3.1. Howard Hughes Medical Institute and Yale University, New Haven, CT.
7. 5 at 2.5 Å resolution. J. Mol. Biol., 184, 279-295.
8. Frazâo, C. et al. (1995) Ab initio determination of the crystal structure of cytochrome c6 and comparison with plastocyanin. Structure, 3, 1159-1169.
9. 1H spin system identification in macromolecules, J. Am. Chem. Soc., 110, 7870-7872.
10. Grzesiek, S. and Bax, A. (1992) Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein. J. Magn. Resonance, 96, 432-440.
11. Güntert, P. and Wüthrich, K. (1992) FLATT - a new procedure for high-quality baseline correction of multidimensional NMR spectra. J. Magn. Resonance, 96, 403-407.
12. Guss, J.M. and Freeman, H.C. (1983) Structure of oxidized poplar plastocyanin at 1.6 Å resolution. J. Mol. Biol., 169, 521-563.
13. Haehnel, W., Jansen, T., Gause, K., Klösgen, R.B., Stahl, B., Michl, D., Huvermann, B., Karas, M. and Herrmann, R.G. (1994) Electron transfer from plastocyanin to photosystem I. EMBO J., 13, 1028-1038.
14. He, S., Modi, S., Bendall, D.S. and Gray, J.C. (1991) The surface-exposed tyrosine residue Tyr83 of pea plastocyanin is involved in both binding and electron transfer reactions with cytochrome f. EMBO J., 10, 4011-4016.
15. Hippler, M., Reichert, J., Sutter, M., Zak, E., Altschmied, L., Schiltz, E., Herrmann, R.G. and Haehnel, W. (1996) The plastocyanin binding domain of plants. EMBO J., 15, 6374-6384.
16. Ho, K.K. and Krogmann, D.W. (1984) Electron donors to P700 in cyanobacteria and algae. An instance of unusual genetic variability. Biochim. Biophys. Acta, 766, 310-316.
17. Holak, T.A., Nilges, M. and Oschkinat, H. (1989) Improved strategies for the determination of protein structures from NMR data: the solution structure of acyl carrier protein. FEBS Lett., 242, 649-654.
18. Hutchinson, E.G. and Thornton, J.M. (1996) PROMOTIF - a program to identify and analyze structural motifs in proteins. Protein Sci., 5, 212-220.
19. 15N spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry, 29, 4659-4667.
20. Jeener, J., Meier, B.H., Bachmann, P. and Ernst, R.R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys., 71, 4546-4553.
21. Kay, L.E., Ikura, M., Tschudin, R. and Bax, A. (1990) Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Resonance, 89, 496-514.
22. 15N NMR spectroscopy. Biochemistry, 35, 7684-7691.
23. Kerfeld, C.A., Haroon, P.A., Interrante, R., Merchant, S. and Yeates, T.O. (1995) The structure of chloroplast cytochrome c6 at 1.9 Å resolution: evidence for functional oligomerization. J. Mol. Biol., 250, 627-647.
24. Kharrat, A., Macias, M.J., Gibson, T.J., Nilges, M. and Pastore, A. (1995) Structure of the dsRNA binding domain of E.coli RNase III. EMBO J., 14, 3572-3584.
25. Kraulis, P. (1991) Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crytallogr., 24, 946-950.
26. Kraulis, P., Clore, G.M., Nilges, M., Jones, T.A., Petterson, G., Knowles, J. and Gronenborn, A.M. (1989) Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry, 28, 7241-7257.
27. Krauß, N., Schubert, W.D., Klukas, O., Fromme, P., Witt, H.T. and Saenger, W. (1996) 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, 965-973.
28. Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
29. Levine, R.L., Mosoni, L., Berlett, B.S. and Stadtman, E.R. (1996) Methionine residues as endogeneous antioxidants in proteins. Proc. Natl Acad. Sci. USA, 93, 15036-15040.
30. 1H spin-spin coupling constants in proteins. Biochem. Biophys. Res. Commun., 113, 967-974.
31. 15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1β. Biochemistry, 28, 6150-6156.
32. Mathews, F.S. (1985) The structure, function and evolution of cytochromes. Prog. Biophys. Mol. Biol., 45, 1-56.
33. Merritt, E.A. and Murphy, M.E.P. (1994) Raster3D version 2.0 - a program for photorealistic molecular graphics. Act. Crystallogr., D50, 869-873.
34. Müller, L. (1979) Sensitivity enhanced detection of weak nuclei using heteronuclear multiple quantum coherence. J. Am. Chem. Soc., 101, 4481-4484.
35. Nicholls, A. (1993) GRASP: Graphical Representation and Analysis of Surface Properties. Columbia University, New York.
36. 1H NMR. Proteins, 17, 297-309.
37. HNα. in a globular protein. J. Mol. Biol., 180, 741-751.
38. Pescheck, G.A. (1996) Cytochrome oxidase and the cta operon of cyanobacteria. Biochim. Biophys. Acta, 1275, 27-32.
39. Powell, M.J.D. (1977) Restart procedures for the conjugate gradient method. Mathemat. Progr., 12, 241-254.
40. Qi, P.X., Di-Stefano, D.L. and Wand, A.J. (1994) Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing. Biochemistry, 33, 6408-6417.
41. 1H NMR spectra of proteins via double quantum filtering. Biochem. Biophys. Res. Commun., 117, 479-485.
42. Richardson, J.S. and Richardson, D.C. (1989) Prediction of Protein Structure and the Principles of Protein Conformation. Plenum Press, New York.
43. Sandmann, G., Reck, H., Kessler, E. and Böger, P. (1983) Distribution of plastocyanin and soluble plastidic cytochrome c in various classes of algae. Arch. Microbiol., 134, 23-27.
44. Sutter, M., Sticht, H., Schmid, R., Hörth, P., Rösch, P. and Haehnel, W. (1995) Cytochrome c6 from the thermophilic Synechococcus elongatus. In Mathis, P. (ed.), Photosynthesis: From Light to Biosphere. Kluwer Academic Publishers, The Netherlands, Vol. II, pp. 563-566.
45. Wagner, G., Braun, W., Havel, T.R. Schaumann, T., Go, N. and Wüthrich, K. (1987) Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using time different algorithms, DISGEO and DISMAN. J. Mol. Biol., 196, 611-639.
46. 1 nitrite reductase. Nature Struct. Biol., 2, 975-982.
47. 13C chemical-shift data. J. Biomol. NMR, 4, 171-180.
48. Wishart, D.S., Sykes, B.D. and Richards, F.M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry, 31, 1647-1651.
49. 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR, 5, 67-81.
50. Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids. John Wiley and Sons, New York.
51. Wüthrich, K., Billeter, M. and Braun, W. (1983) Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J. Mol. Biol., 169, 949-961.
52. Yamaoka, T., Satoh, K. and Katoh, S. (1979) Photosynthetic activities of a thermophilic blue-green alga. Plant Cell Physiol., 19, 943-954.
53. Zuiderweg, E.R.P. and Fesik, S.W. (1989) Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a. Biochemistry, 28, 2387-2391.