메뉴 건너뛰기




Volumn 45, Issue 19, 2006, Pages 6115-6123

Structure of cytochrome c552 from a moderate thermophilic bacterium, Hydrogenophilus thermoluteolus: comparative study on the thermostability of cytochrome c

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; CRYSTAL STRUCTURE; DNA; ELECTROSTATICS; GENETIC ENGINEERING; NUCLEAR MAGNETIC RESONANCE; THERMAL EFFECTS; X RAY ANALYSIS;

EID: 33646543758     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0520131     Document Type: Article
Times cited : (23)

References (38)
  • 1
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke, R., and Böhm, G. (1998) The stability of proteins in extreme environments, Curr. Opin. Struct. Biol. 8, 738-748.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 2
    • 0034717156 scopus 로고    scopus 로고
    • Stability and stabilization of globular proteins in solution
    • Jaenicke, R. (2000) Stability and stabilization of globular proteins in solution, J. Biotechnol. 79, 193-203.
    • (2000) J. Biotechnol. , vol.79 , pp. 193-203
    • Jaenicke, R.1
  • 3
    • 0242290154 scopus 로고    scopus 로고
    • Thermophilic prokaryotes have characteristic patterns of codon usage, amino acid composition and nucleotide content
    • Singer, G. A., and Hickey, D. A. (2003) Thermophilic prokaryotes have characteristic patterns of codon usage, amino acid composition and nucleotide content, Gene 317, 39-47.
    • (2003) Gene , vol.317 , pp. 39-47
    • Singer, G.A.1    Hickey, D.A.2
  • 4
    • 22244450719 scopus 로고    scopus 로고
    • Protein families and their evolution-a structural perspective
    • Orengo, C. A., and Thornton, J. M. (2005) Protein families and their evolution-a structural perspective, Annu. Rev. Biochem. 74, 867-900.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 867-900
    • Orengo, C.A.1    Thornton, J.M.2
  • 5
    • 0036668633 scopus 로고    scopus 로고
    • The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure function relations
    • Bordo, D., and Bork, P. (2002) The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure function relations, EMBO Rep. 3, 741-746.
    • (2002) EMBO Rep. , vol.3 , pp. 741-746
    • Bordo, D.1    Bork, P.2
  • 6
    • 0036373886 scopus 로고    scopus 로고
    • Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability
    • Sambongi, Y., Uchiyama, S., Kobayashi, Y., Igarashi, Y., and Hasegawa, J. (2002) Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability, Eur. J. Biochem. 269, 3355-3361.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3355-3361
    • Sambongi, Y.1    Uchiyama, S.2    Kobayashi, Y.3    Igarashi, Y.4    Hasegawa, J.5
  • 7
    • 0026803109 scopus 로고
    • Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart
    • Kimura, S., Nakamura, H., Hashimoto, T., Oobatake, M., and Kanaya, S. (1992) Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart, J. Biol. Chem. 267, 21535-21542.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21535-21542
    • Kimura, S.1    Nakamura, H.2    Hashimoto, T.3    Oobatake, M.4    Kanaya, S.5
  • 8
    • 0033214040 scopus 로고    scopus 로고
    • Analysis of thermal stabilizing interactions in mesophilic and thermophilic adenylate kinases from the genus Methanococcus
    • Haney, P. J., Stees, M., and Konisky, J. (1999) Analysis of thermal stabilizing interactions in mesophilic and thermophilic adenylate kinases from the genus Methanococcus, J. Biol. Chem. 274, 28453-28458.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28453-28458
    • Haney, P.J.1    Stees, M.2    Konisky, J.3
  • 9
    • 0038690122 scopus 로고    scopus 로고
    • Structures of thermophilic and mesophilic adenylate kinases from the genus Methanococcus
    • Criswell, A. R., Bae, E., Stec, B., Konisky, J., and Phillips, G. N., Jr. (2003) Structures of thermophilic and mesophilic adenylate kinases from the genus Methanococcus, J. Mol. Biol. 330, 1087-1099.
    • (2003) J. Mol. Biol. , vol.330 , pp. 1087-1099
    • Criswell, A.R.1    Bae, E.2    Stec, B.3    Konisky, J.4    Phillips Jr., G.N.5
  • 10
    • 3142653228 scopus 로고    scopus 로고
    • Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases
    • Bae, E., and Phillips, G. N., Jr. (2004) Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases, J. Biol. Chem. 279, 28202-28208.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28202-28208
    • Bae, E.1    Phillips Jr., G.N.2
  • 14
  • 18
    • 1842738707 scopus 로고    scopus 로고
    • Distributed computing and NMR constraint-based high-resolution structure determination: Applied for bioactive peptide endothelin-1 to determine C-terminal folding
    • Takashima, H., Mimura, N., Ohkubo, T., Yoshida, T., Tamaoki, H., and Kobayashi, Y. (2004) Distributed computing and NMR constraint-based high-resolution structure determination: applied for bioactive peptide endothelin-1 to determine C-terminal folding, J. Am. Chem. Soc. 126, 4504-4505.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4504-4505
    • Takashima, H.1    Mimura, N.2    Ohkubo, T.3    Yoshida, T.4    Tamaoki, H.5    Kobayashi, Y.6
  • 19
    • 8344245546 scopus 로고    scopus 로고
    • Hydrophobic core around tyrosine for human endothelin-1 investigated by photochemically induced dynamic nuclear polarization nuclear magnetic resonance and matrix-assisted laser desorption ionization time-of-flight mass spectrometry
    • Takashima, H., Tamaoki, H., Teno, N., Nishi, Y., Uchiyama, S., Fukui, K., and Kobayashi, Y. (2004) Hydrophobic core around tyrosine for human endothelin-1 investigated by photochemically induced dynamic nuclear polarization nuclear magnetic resonance and matrix-assisted laser desorption ionization time-of-flight mass spectrometry, Biochemistry 43, 13932-13936.
    • (2004) Biochemistry , vol.43 , pp. 13932-13936
    • Takashima, H.1    Tamaoki, H.2    Teno, N.3    Nishi, Y.4    Uchiyama, S.5    Fukui, K.6    Kobayashi, Y.7
  • 20
    • 15744367970 scopus 로고    scopus 로고
    • Solution NMR structure investigation for releasing mechanism of neocarzinostatin chromophore from the holoprotein
    • Takashima, H., Yoshida, T., Ishino, T., Hasuda, K., Ohkubo, T., and Kobayashi, Y. (2005) Solution NMR structure investigation for releasing mechanism of neocarzinostatin chromophore from the holoprotein, J. Biol. Chem. 280, 11340-11346.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11340-11346
    • Takashima, H.1    Yoshida, T.2    Ishino, T.3    Hasuda, K.4    Ohkubo, T.5    Kobayashi, Y.6
  • 21
    • 0031971555 scopus 로고    scopus 로고
    • Heterologous expression of Hydrogenobacter thermophilus cytochrome c-552 in the periplasm of Pseudomonas aeruginosa
    • Zhang, Y., Arai, H., Sambongi, Y., Igarashi, Y., and Kodama, T. (1998) Heterologous expression of Hydrogenobacter thermophilus cytochrome c-552 in the periplasm of Pseudomonas aeruginosa, J. Ferment. Bioeng. 85, 346-349.
    • (1998) J. Ferment. Bioeng. , vol.85 , pp. 346-349
    • Zhang, Y.1    Arai, H.2    Sambongi, Y.3    Igarashi, Y.4    Kodama, T.5
  • 22
    • 15044352651 scopus 로고    scopus 로고
    • CD measurement of aqueous protein solution at high temperature up to 180°C-Thermodynamic analysis of thermophilic protein by pressure-proof cell compartment
    • Ohshima, A., Uchiyama, S., Nakano, H., Yoshida, T., Ohkubo, T., and Kobayashi, Y. (2003) CD measurement of aqueous protein solution at high temperature up to 180°C-Thermodynamic analysis of thermophilic protein by pressure-proof cell compartment, Lett. Pept. Sci. 10, 539-543.
    • (2003) Lett. Pept. Sci. , vol.10 , pp. 539-543
    • Ohshima, A.1    Uchiyama, S.2    Nakano, H.3    Yoshida, T.4    Ohkubo, T.5    Kobayashi, Y.6
  • 24
    • 0023406843 scopus 로고
    • Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves
    • Marky, L. A., and Breslauer, K. J. (1987) Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves, Biopolymers 26, 1601-1620.
    • (1987) Biopolymers , vol.26 , pp. 1601-1620
    • Marky, L.A.1    Breslauer, K.J.2
  • 25
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro, M. M., and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants, Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 26
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath, J. W. (1999) The finer things in X-ray diffraction data collection, Acta Crystallogr. D55, 1718-1725.
    • (1999) Acta Crystallogr. , vol.D55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 27
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A., and Teplyakov, A. (1997) MOLREP: An automated program for molecular replacement, Acta Crystallogr. D30, 1022-1025.
    • (1997) Acta Crystallogr. , vol.D30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 30
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. (1999) XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density, J. Struct. Biol. 125, 156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 31
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • 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.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 32
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983) Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features, Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 33
    • 33646583759 scopus 로고    scopus 로고
    • Martin, A. C. R. (1996) ProFit, http://www.bioinf.org.uk/software/profit/ .
    • (1996) ProFit
    • Martin, A.C.R.1
  • 35
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 37
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati, V. (1952) Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallogr. 5, 802-810.
    • (1952) Acta Crystallogr. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 38
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of alpha helices
    • Richardson, J. S., and Richardson, D. C. (1988) Amino acid preferences for specific locations at the ends of alpha helices, Science 240, 1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.