Solution structure of ferredoxin from the thermophilic cyanobacterium Synechococcus elongatus and its thermostability

Journal of Molecular Biology

Volumn 268, Issue 5, 1997, Pages 922-933

  Hatanaka, Hideki ^a   Tanimura, Ryuji ^b   Katoh, Sakae ^c,d   Inagaki, Fuyuhiko ^a  

^a TOKYO METROPOLITAN INSTITUTE OF MEDICAL SCIENCE   (Japan)

^b TORAY INDUSTRIES INC   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

^d TOHO UNIVERSITY   (Japan)

Author keywords

Distance geometry; Ferredoxin; Nuclear magnetic resonance; Thermostability; Three dimensional structure

Indexed keywords

FERREDOXIN;

ARTICLE; CRYSTAL STRUCTURE; CYANOBACTERIUM; GRAM NEGATIVE BACTERIUM; HYDROPHOBICITY; NONHUMAN; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; THERMOSTABILITY;

EID: 0031584272     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1001     Document Type: Article

References (51)

1. Abola E. E., Bernstein F. C., Bryant S. H., Koetzle T. F., Weng J. Protein data bank. Crystallographic Databases-Information Content, Software Systems, Scientific Applications. 1987;Data Commission of the International Union of Crystallography, Bonn, Cambridge, Chester.
2. Alam J., Whitaker R. A., Krogmann D. W., Curtis S. E. Isolation and sequence of the gene for ferredoxin I from the cyanobacteriumAnabaena. J. Bacteriol. 168:1986;1265-1271.
3. 22. Biochemistry. 35:1996;12831-12841.
4. Bax A., Davis D. G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:1985;355-360.
5. Bernstein F. C., Koetzle T. F., Williams G. J. B., Meyer E. F. Jr, Brice M. D., Rodgers J. R., Kennard O., Shimanouchi T., Tasumi M. The Protein Data Bank; a computer-based archival file for macromolecular structures. J. Mol. Biol. 112:1977;535-542.
6. Böhme H., Haselkorn R. Molecular cloning and nucleotide sequence analysis of the gene coding for heterocyst ferredoxin from the cyanobacteriumAnabaena. Mol. Gen. Genet. 214:1988;278-285.
7. Borden D., Margoliash E. PIR Data Bank (accession number A00258). 1979.
8. Brant D. A., Shimmel P. R. Analysis of the skeletal configuration of crystalline hen egg-white lysozyme. Proc. Natl Acad. Sci. USA. 58:1967;428-435.
9. Brooks B. R., Bruccoleri R. E., Olafson B. D., States D. J., Swaminathan S., Karplus M. CHARMm: a program for macromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 4:1983;187-217.
10. Brünger A. T. X-PLOR Version 3.1: A System for X-Ray Crystallography and NMR. 1993;Yale University Press, New Haven, CT.
11. Cavanagh J., Rance M. Suppression of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence. J. Magn. Reson. 96:1992;670-678.
12. Chae Y. K., Abildgaard F., Mooberry E. S., Markley J. L. Multinuclear, multidimensional NMR studies ofAnabaena 7120. Biochemistry. 33:1994;3287-3295.
13. Frolow F., Harel M., Sussman J. L., Mevarech M., Shoham M. Insights into protein adaptation to a saturated salt environment from the crystal structure of halophilic 2Fe-2S ferredoxin. Nature Struct. Biol. 3:1996;452-458.
14. Fukuyama K., Hase T., Matsumoto S., Tsukihara T., Katsube Y., Tanaka N., Kakudo M., Wada K., Matsubara H. Structure ofSpirulina platensis. Nature. 286:1980;522-524.
15. Fukuyama K., Ueki N., Nakamura H., Tsukihara T., Matsubara H. Tertiary structure of [2Fe-2S] ferredoxin fromSpirulina platensis. J. Biochem. 117:1995;1017-1023.
16. Hase T., Wada K., Matsubara H. Amino acid sequence of the major component ofAphanothece sacrum. J. Biochem. 79:1976a;329-343.
17. Hase T., Ohmiya N., Matsubara H., Mullinger R. N., Rao K. K., Hall D. O. Amino acid sequence of a four-iron-four-sulphur ferredoxin isolated fromBacillus stearothermophilus. Biochem. J. 159:1976b;55-63.
18. Hase T., Wada K., Matsubara H. Horsetail (Equisetum arvense. J. Biochem. 82:1977;277-286.
19. Hase T., Wakabayashi S., Matsubara H., Rao K. K., Hall D. O., Widmer H., Gysi J., Zuber H. The amino acid sequence of ferredoxin from the algaMastigocladus laminosus. Phytochemistry. 17:1978a;1863-1867.
20. Hase T., Wakabayashi S., Matsubara H., Jüttner F., Rao K. K., Fry I., Hall D. O. Cyanidium caldarium. FEBS Letters. 96:1978b;41-44.
21. Hase T., Matsubara H., Koike H., Katoh S. Amino acid sequence of ferredoxin from a thermophilic blue-green alga,Synechococcus. Biochim. Biophys. Acta. 744:1983;46-52.
22. Hatanaka H., Oka M., Kohda D., Tate S., Suda A., Tamiya N., Inagaki F. Tertiary structure of erabutoxin b in aqueous solution as elucidated by two-dimensional nuclear magnetic resonance. J. Mol. Biol. 240:1994;155-166.
23. Hatanaka H., Ogura K., Moriyama K., Ichikawa S., Yahara I., Inagaki F. Tertiary structure of destrin and structural similarity between two-regulating protein families. Cell. 85:1996;1047-1055.
24. Holden H. M., Jacobson B. L., Hurley J. K., Tollin G., Oh B. H., Skjeldal L., Chae Y. K., Cheng H., Xia B., Markley J. L. Structure-function studies of [2Fe-2S] ferredoxins. J. Bioenerg. Biomemb. 26:1994;67-88.
25. Hurley J. K., Caffrey M. S., Markley J. L., Cheng H., Xia B., Chae Y. K., Tollin G. Mutations of surface residues inAnabaena. Protein Sci. 4:1995;58-64.
26. Ikemizu S., Bando M., Sato T., Morimoto S., Tsukihara T., Katsube Y., Tanaka N., Kakudo M., Wada K., Matsubara H. Crystal structure of [2Fe-2S] ferredoxin I fromEquisetum Arvense. Acta Crystallog. sect. D. 50:1994;167-174.
27. Jacobson B. L., Chae Y. K., Markley J. L., Rayment I., Holden H. M. Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin fromAnabaena. Biochemistry. 32:1993;6788-6793.
28. Jeener J., Meier B. H., Bachmann P., Ernst R. R. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71:1979;4546-4553.
29. Knaff D. B., Hirasawa M. Ferredoxin-dependent chloroplast enzymes. Biochim. Biophys. Acta. 1056:1991;93-125.
30. Kohda D., Inagaki F. Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions. Biochemistry. 31:1992;11928-11939.
31. Kohda D., Terasawa H., Ichikawa S., Ogura K., Hatanaka H., Mandiyan V., Ullrich A., Schlessinger J., Inagaki F. Solution structure and ligand-binding site of the carboxy-terminal SH3 domain of GRB2. Structure. 2:1994;1029-1040.
32. Koike H., Katoh S. Heat-stabilities of cytochromes and ferredoxin isolated from a thermophilic blue-green alga. Plant Cell Physiol. 20:1979;1157-1161.
33. Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
34. Krauss N., Hinrichs W., Witt I., Fromme P., Pritzlow W., Dauter Z., Betzel C., Wilson K. S., Witt H. T., Saenger W. Three-dimensional structure of system I of photosynthesis at 6 Å resolution. Nature. 361:1993;326-331.
35. 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 anttena system. Nature Struct. Biol. 3:1996;965-973.
36. Macura S., Huang Y., Suter D., Ernst R. R. Two-dimensional chemical exchange and cross-relaxation spectroscopy of coupled nuclear spins. J. Magn. Reson. 43:1981;259-281.
37. Matthews B. W. Structural and genetic analysis of protein stability. Annu. Rev. Biochem. 62:1993;139-160.
38. Nilges M., Clore G. M., Gronenborn A. M. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Letters. 229:1988;317-324.
39. Oh B.-H., Markley J. L. Multinuclear magnetic resonance studies of the 2Fe·2S* ferredoxin fromAnabaena. Biochemistry. 29:1990;3993-4004.
40. Perutz M. F., Raidt H. Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2. Nature. 255:1975;256-259.
41. Pochapsky T. C., Ye X. M., Ratnaswamy G., Lyons T. A. An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin fromPseudomonas. Biochemistry. 33:1994;6424-6432.
42. Rance M., Sørensen O. W., Bodenhausen G., Wagner G., Ernst R. R., Wüthrich K. Improved spectral resolution in COSY proton NMR spectra of proteinsvia. Biochem. Biophys. Res. Commun. 117:1983;479-485.
43. Rypniewski W. R., Breiter D. R., Benning M. M., Wesenberg G., Oh B.-H., Markley J. L., Rayment I., Holden H. M. Crystallization and structure determination to 2.5 Å resolution of the oxidized [2Fe-2S] ferredoxin isolated fromAnabaena. Biochemistry. 30:1991;4126-4131.
44. States D. J., Haberkorn R. A., Ruben D. J. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J. Magn. Reson. 48:1982;286-292.
45. Tanaka M., Haniu M., Yasunobu K. T., Himes R. H., Akagi J. M. The primary structure of theClostridium thermosaccharolyticum. J. Biol. Chem. 248:1973;5215-5217.
46. Tanaka M., Haniu M., Yasunobu K. T., Rao K. K., Hall D. O. The complete amino acid sequence of theSpirulina platensis. Biochem. Biophys. Res. Commun. 69:1976;759-765.
47. Tsukihara T., Fukuyama K., Nakamura M., Katsube Y., Tanaka N., Kakudo M., Wada K., Hase T., Matsubara H. X-ray analysis of a [2Fe-2S] ferredoxin fromSpirulina platensis. J. Biochem. 90:1981;1763-1773.
48. Tsukihara T., Fukuyama K., Mizushima M., Harioka T., Kusunoki M., Katsube Y., Hase T., Matsubara H. Structure of the [2Fe-2S] ferredoxin I from the blue-green algaAphanothece sacrum. J. Mol. Biol. 216:1990;399-410.
49. Tsutsui T., Tsukihara T., Fukuyama K., Katsube Y., Hase T., Wada K., Matsubara H., Nishikawa Y., Tanaka N. Main chain fold of a [2Fe-2S] ferredoxin I fromAphanothece sacrum. J. Biochem. 94:1983;299-302.
50. Wüthrich K. NMR of Proteins and Nucleic Acids. 1986;John Wiley, New York.
51. 2. J. Magn. Reson. 70:1986;336-343.