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Volumn 128, Issue 1, 2000, Pages 113-119

Tryptophan 140 is important, but Serine 141 is essential for the formation of the integrated conformation of staphylococcal nuclease

Author keywords

N terminal fragment; Peptide folding; Staphylococcal nuclease

Indexed keywords

BACTERIAL ENZYME; NUCLEASE; SERINE; TRYPTOPHAN;

EID: 0033914528     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022721     Document Type: Article
Times cited : (13)

References (29)
  • 1
    • 0024316597 scopus 로고
    • 2+, and the inhibitor pdTp, refined at 1.65 Å
    • 2+, and the inhibitor pdTp, refined at 1.65 Å. Proteins 5, 183-201
    • (1989) Proteins , vol.5 , pp. 183-201
    • Loll, P.J.1    Lattman, E.E.2
  • 2
    • 0025877987 scopus 로고
    • The crystal structure of staphylococcal nuclease refined at 1.7 Å resolution
    • Hynes, T.R. and Fox, P.O. (1991) The crystal structure of staphylococcal nuclease refined at 1.7 Å resolution. Proteins 10, 92-105
    • (1991) Proteins , vol.10 , pp. 92-105
    • Hynes, T.R.1    Fox, P.O.2
  • 3
    • 0022994226 scopus 로고
    • Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrocbloride and urea denaturation
    • Shortle, D. and Meeker, A.K. (1986) Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrocbloride and urea denaturation. Proteins 1, 81-89
    • (1986) Proteins , vol.1 , pp. 81-89
    • Shortle, D.1    Meeker, A.K.2
  • 4
    • 0022571680 scopus 로고
    • Guanidine hydrochloride denaturation studies of mutant forms of staphylococcal nuclease
    • Shortle, D. (1986) Guanidine hydrochloride denaturation studies of mutant forms of staphylococcal nuclease. J. Cell. Biochem. 30, 281-289
    • (1986) J. Cell. Biochem. , vol.30 , pp. 281-289
    • Shortle, D.1
  • 5
    • 0024550047 scopus 로고
    • Probing the determinants of protein folding and stability with amino acid substitutions
    • Shortle, D. (1989) Probing the determinants of protein folding and stability with amino acid substitutions. J. Biol. Chem. 264, 5313-5318
    • (1989) J. Biol. Chem. , vol.264 , pp. 5313-5318
    • Shortle, D.1
  • 6
    • 0024965951 scopus 로고
    • A magnetization-transfer nuclear magnetic resonance study of the folding of staphylococcal nuclease
    • Evans, P.A., Kautz, R.A., Fox, R.O., and Dobson, C.M. (1989) A magnetization-transfer nuclear magnetic resonance study of the folding of staphylococcal nuclease. Biochemistry 28, 362-370
    • (1989) Biochemistry , vol.28 , pp. 362-370
    • Evans, P.A.1    Kautz, R.A.2    Fox, R.O.3    Dobson, C.M.4
  • 7
    • 0025911196 scopus 로고
    • Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra
    • Sugawara, T., Kuwajima, K., and Sugai, S. (1991) Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra. Biochemistry 30, 2698-2706
    • (1991) Biochemistry , vol.30 , pp. 2698-2706
    • Sugawara, T.1    Kuwajima, K.2    Sugai, S.3
  • 8
    • 0004282486 scopus 로고
    • NaCl-induced conformational transition of the acid-unfolded state of staphylococcal nuclease
    • Bi, X.P., Jiang, M.Y., and Jing, G.Z. (1995) NaCl-induced conformational transition of the acid-unfolded state of staphylococcal nuclease. Sci. China (Ser. B) 38, 1222-1229
    • (1995) Sci. China (Ser. B) , vol.38 , pp. 1222-1229
    • Bi, X.P.1    Jiang, M.Y.2    Jing, G.Z.3
  • 9
    • 0024963569 scopus 로고
    • Residual structure in large fragments of staphylococcal nuclease: Effects of amino acid substitutions
    • Shortle, D. and Meeker, A.K. (1989) Residual structure in large fragments of staphylococcal nuclease: Effects of amino acid substitutions. Biochemistry 28, 936-944
    • (1989) Biochemistry , vol.28 , pp. 936-944
    • Shortle, D.1    Meeker, A.K.2
  • 11
    • 0030066904 scopus 로고    scopus 로고
    • Mapping the structure of a non-native state of staphylococcal nuclease
    • Ermacora, M.R., Ledman, D.W., and Fox, R.O. (1996) Mapping the structure of a non-native state of staphylococcal nuclease. Nat. Struct. Biol. 3, 59-66
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 59-66
    • Ermacora, M.R.1    Ledman, D.W.2    Fox, R.O.3
  • 12
    • 0027918159 scopus 로고
    • NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease
    • Shortle, D. and Abeyguanawardana, C. (1993) NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease. Structure 15, 127-134
    • (1993) Structure , vol.15 , pp. 127-134
    • Shortle, D.1    Abeyguanawardana, C.2
  • 13
    • 0026602010 scopus 로고
    • High level expression of staphylococcal nuclease R gene in Escherichia coli
    • Jing, G.Z., Liu, L.J., Jiang, M.Y., Zou, Q., and He, R.Q. (1992) High level expression of staphylococcal nuclease R gene in Escherichia coli. J. Biotechnol. 22, 271-282
    • (1992) J. Biotechnol. , vol.22 , pp. 271-282
    • Jing, G.Z.1    Liu, L.J.2    Jiang, M.Y.3    Zou, Q.4    He, R.Q.5
  • 14
    • 0032420786 scopus 로고    scopus 로고
    • Conformational features of a truncated staphylococcal nuclease R (SNR135) and their implications for catalysis
    • Zhou, B. and Jing, G.Z. (1998) Conformational features of a truncated staphylococcal nuclease R (SNR135) and their implications for catalysis. Arch. Biochem. Biophys. 360, 33-40
    • (1998) Arch. Biochem. Biophys. , vol.360 , pp. 33-40
    • Zhou, B.1    Jing, G.Z.2
  • 15
    • 0033970156 scopus 로고    scopus 로고
    • An in vitro peptide folding model suggests the presence of the molten globule state during nascent peptide folding
    • Zhou, B., Tian, K.G., and Jing, G.Z. (2000) An in vitro peptide folding model suggests the presence of the molten globule state during nascent peptide folding. Protein Eng. 13, 35-39
    • (2000) Protein Eng. , vol.13 , pp. 35-39
    • Zhou, B.1    Tian, K.G.2    Jing, G.Z.3
  • 16
    • 0029795957 scopus 로고    scopus 로고
    • Unfolding and refolding of N-terminal fragments of staphylococcal nuclease R in guanidine hydrochloride
    • Zhou, B. and Jing, G.Z. (1996) Unfolding and refolding of N-terminal fragments of staphylococcal nuclease R in guanidine hydrochloride. J. Biochem. 120, 881-888
    • (1996) J. Biochem. , vol.120 , pp. 881-888
    • Zhou, B.1    Jing, G.Z.2
  • 17
    • 0031718155 scopus 로고    scopus 로고
    • Folding of SNase R begins early during synthesis: The conformational feature of two short N-terminal fragments of staphylococcal nuclease R
    • Tian, K.G., Zhou, B., Geng, F.G., and Jing, G.Z. (1998) Folding of SNase R begins early during synthesis: The conformational feature of two short N-terminal fragments of staphylococcal nuclease R. Int. J. Biol. Macromol. 23, 199-206
    • (1998) Int. J. Biol. Macromol. , vol.23 , pp. 199-206
    • Tian, K.G.1    Zhou, B.2    Geng, F.G.3    Jing, G.Z.4
  • 18
    • 0029134918 scopus 로고
    • Comparative studies of the conformation of the N-terminal fragments of staphylococcal nuclease R in solution
    • Jing, G.Z., Zhou, B., Xie, L., and Liu, Z.G. (1995) Comparative studies of the conformation of the N-terminal fragments of staphylococcal nuclease R in solution. Biochim. Biophys. Acta 1250, 189-196
    • (1995) Biochim. Biophys. Acta , vol.1250 , pp. 189-196
    • Jing, G.Z.1    Zhou, B.2    Xie, L.3    Liu, Z.G.4
  • 19
    • 85037962129 scopus 로고    scopus 로고
    • Trp140 and structural integrity of the helices and the active site of staphylococcal nuclease
    • May 7-10, Guilin, China, Chinese Society of Biochemistry & Molecular Biology, China
    • Hu, H.Y., Ao, W.Y., and Tsong, T.Y. (1998) Trp140 and structural integrity of the helices and the active site of staphylococcal nuclease in International Symposium - Mechanisms of Enzymatic Catalysis, May 7-10, Guilin, China, pp. 47-48, Chinese Society of Biochemistry & Molecular Biology, China
    • (1998) International Symposium - Mechanisms of Enzymatic Catalysis , pp. 47-48
    • Hu, H.Y.1    Ao, W.Y.2    Tsong, T.Y.3
  • 20
    • 21944441493 scopus 로고    scopus 로고
    • Determination of protein extinction coefficients by alkaline hydrolysis
    • Zhou, B. and Jing, G.Z. (1999) Determination of protein extinction coefficients by alkaline hydrolysis (in Chinese). Progr. Biochem. Biophys. 26, 384-387
    • (1999) Progr. Biochem. Biophys. , vol.26 , pp. 384-387
    • Zhou, B.1    Jing, G.Z.2
  • 21
    • 0014198139 scopus 로고
    • Catalytic properties and specificity of the extracellular nuclease of Staphylococcus aureus
    • Cuatrecasas, P., Fuchs, S., and Anfinsen, C.B. (1967) Catalytic properties and specificity of the extracellular nuclease of Staphylococcus aureus. J. Biol. Chem. 242, 1541-1547
    • (1967) J. Biol. Chem. , vol.242 , pp. 1541-1547
    • Cuatrecasas, P.1    Fuchs, S.2    Anfinsen, C.B.3
  • 22
    • 0028143230 scopus 로고
    • Residual structure in a staphylococcal nuclease fragments
    • Griko, Y.V., Gitts, A., Lattman, E.E., and Privalov, P.L. (1994) Residual structure in a staphylococcal nuclease fragments. J. Mol. Biol. 243, 93-99
    • (1994) J. Mol. Biol. , vol.243 , pp. 93-99
    • Griko, Y.V.1    Gitts, A.2    Lattman, E.E.3    Privalov, P.L.4
  • 23
    • 0000261801 scopus 로고
    • Staphylococcal nuclease: Proposed mechanism of action based on structure of enzyme-thymidine 3′,5′-bisphosphate-calcium ion complex at 1.5 Å
    • Cotton, F.A., Hazen, E.E., and Legg, M.J. (1979) Staphylococcal nuclease: proposed mechanism of action based on structure of enzyme-thymidine 3′,5′-bisphosphate-calcium ion complex at 1.5 Å. Proc. Natl. Acad. Sci. USA 76, 2551-2555
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2551-2555
    • Cotton, F.A.1    Hazen, E.E.2    Legg, M.J.3
  • 25
    • 0028125665 scopus 로고
    • Comparison of kinetics of formation of helices and hydrophobic core during the folding of staphylococcal nucleases from acid
    • Chen, H.M. and Tsong, T.Y. (1994) Comparison of kinetics of formation of helices and hydrophobic core during the folding of staphylococcal nucleases from acid. Biophys. J. 66, 40-45
    • (1994) Biophys. J. , vol.66 , pp. 40-45
    • Chen, H.M.1    Tsong, T.Y.2
  • 26
    • 0024294294 scopus 로고
    • Folding of the nascent chain into a biological active protein
    • Tsou, C.L. (1988) Folding of the nascent chain into a biological active protein. Biochemistry 27, 1809-1812
    • (1988) Biochemistry , vol.27 , pp. 1809-1812
    • Tsou, C.L.1
  • 27
    • 0028274250 scopus 로고
    • Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study
    • Alexandrescu, A.T., Abeygunawardana, C., and Shortle, D. (1994) Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study. Biochemistry 33, 1063-1072
    • (1994) Biochemistry , vol.33 , pp. 1063-1072
    • Alexandrescu, A.T.1    Abeygunawardana, C.2    Shortle, D.3
  • 28
    • 0031565731 scopus 로고    scopus 로고
    • Comprehensive NOE characterization of a partially folded large fragment of staphylococcal nuclease Δ131Δ, using NMR methods with improved resolution
    • Zhang, O., Kay, L.E., Shortle, D., and Forman-Kay, J.D. (1997) Comprehensive NOE characterization of a partially folded large fragment of staphylococcal nuclease Δ131Δ, using NMR methods with improved resolution. J. Mol. Biol. 272, 9-20
    • (1997) J. Mol. Biol. , vol.272 , pp. 9-20
    • Zhang, O.1    Kay, L.E.2    Shortle, D.3    Forman-Kay, J.D.4
  • 29
    • 0242568809 scopus 로고    scopus 로고
    • Analysis on the crystal structure of the N-terminal fragments (SNR141) of staphylococcal nuclease refined at 1.9 Å
    • Yang, Z., Ye, S. Jing, G.Z., Gui, L.L., and Liang, D.C. (1999) Analysis on the crystal structure of the N-terminal fragments (SNR141) of staphylococcal nuclease refined at 1.9 Å (in Chinese). Progr. Nat. Sci. 9, 595-601
    • (1999) Progr. Nat. Sci. , vol.9 , pp. 595-601
    • Yang, Z.1    Ye, S.2    Jing, G.Z.3    Gui, L.L.4    Liang, D.C.5


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