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Volumn 3, Issue 5, 1996, Pages 452-458

Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin

Author keywords

[No Author keywords available]

Indexed keywords

FERREDOXIN; IRON SULFUR PROTEIN; SODIUM CHLORIDE;

EID: 0030010138     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0596-452     Document Type: Review
Times cited : (191)

References (22)
  • 2
    • 0026646179 scopus 로고
    • Biochemical, structural, and molecular genetic aspects of halophilism
    • Eisenberg, H., Mevarech, M. & Zaccai, G. Biochemical, structural, and molecular genetic aspects of halophilism. Adv. Prot Chem. 43, 1-62 (1992).
    • (1992) Adv. Prot Chem. , vol.43 , pp. 1-62
    • Eisenberg, H.1    Mevarech, M.2    Zaccai, G.3
  • 3
    • 0028314679 scopus 로고
    • Structure-function studies of [2Fe-2S] ferredoxins
    • Holden, H.M. et al. Structure-function studies of [2Fe-2S] ferredoxins J. Bioenerg. Biomembr. 26, 67-88 (1994).
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 67-88
    • Holden, H.M.1
  • 4
    • 0020352834 scopus 로고
    • Structure-function relationship of [2Fe-2S] ferredoxins and design of a model molecule
    • Tsukihara, T. et al. Structure-function relationship of [2Fe-2S] ferredoxins and design of a model molecule, BioSystems 15, 243-257 (1982).
    • (1982) BioSystems , vol.15 , pp. 243-257
    • Tsukihara, T.1
  • 5
    • 0344366698 scopus 로고
    • Expression of human ferredoxin and assembly of the [2Fe-2S] center in Escherichia coli
    • Coghlan, V.M. & Vickery, L.E. Expression of human ferredoxin and assembly of the [2Fe-2S] center in Escherichia coli. Proc. Natl. Acad. Sci. USA 86, 835-839 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 835-839
    • Coghlan, V.M.1    Vickery, L.E.2
  • 6
    • 0028958071 scopus 로고
    • Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium
    • Dym, O., Mevarech, M. & Sussman, J.L. Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium. Science 267, 1344-1346 (1995).
    • (1995) Science , vol.267 , pp. 1344-1346
    • Dym, O.1    Mevarech, M.2    Sussman, J.L.3
  • 7
    • 0017872059 scopus 로고
    • Purification and characterization of a highly acidic 2Fe-ferredoxin from Halobacterium of the Dead Sea
    • Werber, M.M., & Mevarech, M. Purification and characterization of a highly acidic 2Fe-ferredoxin from Halobacterium of the Dead Sea. Arch. Bioch. Biophys. 187, 447-456 (1978).
    • (1978) Arch. Bioch. Biophys. , vol.187 , pp. 447-456
    • Werber, M.M.1    Mevarech, M.2
  • 8
    • 0015241654 scopus 로고
    • Hydration of macromolecules. IV. Polypeptide conformation in frozen solutions
    • Kuntz, I.D. Hydration of macromolecules. IV. Polypeptide conformation in frozen solutions. J. Am. Chem. Soc. 93, 516-518 (1971).
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 516-518
    • Kuntz, I.D.1
  • 9
    • 0028013478 scopus 로고
    • Thermal expansion of hen egg-white lysozyme. Comparison of the 1.9 Å resolution structures of the teragonal form of the enzyme at 100° K and 298° K
    • Young, A.C., Tilton, R.F. & Dewan, J. C. Thermal expansion of hen egg-white lysozyme. Comparison of the 1.9 Å resolution structures of the teragonal form of the enzyme at 100° K and 298° K. J. Mol. Biol. 235, 302-317 (1994).
    • (1994) J. Mol. Biol. , vol.235 , pp. 302-317
    • Young, A.C.1    Tilton, R.F.2    Dewan, J.C.3
  • 10
    • 0025907697 scopus 로고
    • Crystallization and structure determination to 2.5 Å resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120
    • Rypniewski, W.R. et al. Crystallization and structure determination to 2.5 Å resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120, Biochemistry 30, 4126-5131 (1991).
    • (1991) Biochemistry , vol.30 , pp. 4126-5131
    • Rypniewski, W.R.1
  • 11
    • 0027301957 scopus 로고
    • Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120 determined to 1.7 Å resolution
    • Jacobson, B.L., Chae, Y.K., Markley, J.L., Rayment, I. & Holden, H. M. Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120 determined to 1.7 Å resolution. Biochemistry 32, 6788-6793. (1993).
    • (1993) Biochemistry , vol.32 , pp. 6788-6793
    • Jacobson, B.L.1    Chae, Y.K.2    Markley, J.L.3    Rayment, I.4    Holden, H.M.5
  • 12
    • 0025607113 scopus 로고
    • Structure of the [2Fe-2S] ferredoxin I from the blue-green alga Aphanothece sacrum at 2.2 Å resolution
    • Tsukihara, T. et al. Structure of the [2Fe-2S] ferredoxin I from the blue-green alga Aphanothece sacrum at 2.2 Å resolution. J. Mol. Biol. 216, 399-410 (1990).
    • (1990) J. Mol. Biol. , vol.216 , pp. 399-410
    • Tsukihara, T.1
  • 13
    • 0019739089 scopus 로고
    • X-ray analysis of a [2Fe-2S] ferredoxin from Sprirulina platensis. Main chain fold and location of side chains at 2.5 Å resolution
    • Tsukihara, T. et al. X-ray analysis of a [2Fe-2S] ferredoxin from Sprirulina platensis. Main chain fold and location of side chains at 2.5 Å resolution. J. Biochem. 90, 1763-1773 (1981).
    • (1981) J. Biochem. , vol.90 , pp. 1763-1773
    • Tsukihara, T.1
  • 14
    • 0028042530 scopus 로고
    • Structure of [2Fe-2S] ferredoxin I from Equisetum arvense at 1.8 Å resolution
    • Ikemizu, S., Bando, M., Sato, T., Morimoto, Y. & Tsukihara, T. Structure of [2Fe-2S] ferredoxin I from Equisetum arvense at 1.8 Å resolution. Acta Crystallogr. D50, 167-174 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 167-174
    • Ikemizu, S.1    Bando, M.2    Sato, T.3    Morimoto, Y.4    Tsukihara, T.5
  • 15
    • 0018801416 scopus 로고
    • Preliminary X-ray diffraction studies on 2Fe-ferredoxin from Halobacterium of the Dead Sea
    • Sussman, J.L., Zipori, P., Harel, M., Yonath, A. & Werber, M.M. Preliminary X-ray diffraction studies on 2Fe-ferredoxin from Halobacterium of the Dead Sea, J. Mol. Biol. 134, 375-377 (1979).
    • (1979) J. Mol. Biol. , vol.134 , pp. 375-377
    • Sussman, J.L.1    Zipori, P.2    Harel, M.3    Yonath, A.4    Werber, M.M.5
  • 16
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones, A. A graphics model building and refinement system for macromolecules. J. Appl. Crystallogr. 11, 268-272 (1978).
    • (1978) J. Appl. Crystallogr. , vol.11 , pp. 268-272
    • Jones, A.1
  • 17
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119 (1991).
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 19
    • 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. Bioploymers 22, 2577-2637 (1983).
    • (1983) Bioploymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 22
    • 0023053742 scopus 로고
    • Phosphocholine binding immunoglobulin Fab McP603. An X-ray diffraction study at 2.7 Å
    • Satow, Y., Cohen, G.H., Padlan, E.A. & Davies, D.R. Phosphocholine binding immunoglobulin Fab McP603. An X-ray diffraction study at 2.7 Å. J. Mol. Biol. 190, 593-604 (1986).
    • (1986) J. Mol. Biol. , vol.190 , pp. 593-604
    • Satow, Y.1    Cohen, G.H.2    Padlan, E.A.3    Davies, D.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.