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Volumn 259, Issue 1, 1996, Pages 148-159

Context dependence of mutational effects in a protein: The crystal structures of the V35I, I47V and V35I/I47V gene V protein core mutants

Author keywords

Filamentous phage; Gene V protein; Protein stability; Site specific mutants; X ray crystallography

Indexed keywords

AMINO ACID; DIMER; ISOLEUCINE;

EID: 0029984120     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0309     Document Type: Article
Times cited : (21)

References (52)
  • 1
    • 0027716138 scopus 로고
    • The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme
    • Baldwin, E. P., Hajiseyedjavadi, O., Baase, W. A. & Matthews, B. W. (1993). The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. Science, 262, 1715-1718.
    • (1993) Science , vol.262 , pp. 1715-1718
    • Baldwin, E.P.1    Hajiseyedjavadi, O.2    Baase, W.A.3    Matthews, B.W.4
  • 3
    • 0004283186 scopus 로고
    • Department of Molecular Biophysics & Biochemistry Yale University, New Haven, CT
    • Brünger, A. T. (1992). X-PLOR 3.1. Department of Molecular Biophysics & Biochemistry Yale University, New Haven, CT.
    • (1992) X-PLOR 3.1
    • Brünger, A.T.1
  • 4
    • 0027133653 scopus 로고
    • Crystal structural analysis of mutations in the hydrophobic cores of barnase
    • Buckle, A. M., Henrick, K. & Fersht, A. R. (1993). Crystal structural analysis of mutations in the hydrophobic cores of barnase. J. Mol. Biol. 234, 847-860.
    • (1993) J. Mol. Biol. , vol.234 , pp. 847-860
    • Buckle, A.M.1    Henrick, K.2    Fersht, A.R.3
  • 5
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson, M. (1987). Ribbon models of macromolecules. J. Mol. Graph. 5, 103-106.
    • (1987) J. Mol. Graph. , vol.5 , pp. 103-106
    • Carson, M.1
  • 6
    • 0014885326 scopus 로고
    • Conformation of amino acids. XI. Analysis of the observed side group conformations in proteins
    • Chandrasekaran, R. & Ramachandran, G. N. (1970). Conformation of amino acids. XI. Analysis of the observed side group conformations in proteins. Int. J. Protein Res. 2, 223-233.
    • (1970) Int. J. Protein Res. , vol.2 , pp. 223-233
    • Chandrasekaran, R.1    Ramachandran, G.N.2
  • 7
    • 0029137933 scopus 로고
    • Crystallographic analysis of Phe-Leu substitution in the hydrophobic core of barnase
    • Chen, Y. W., Fersht, A. R. & Henrick, K. (1995). Crystallographic analysis of Phe-Leu substitution in the hydrophobic core of barnase. Acta Crystallog. sect. D, 51, 220-231.
    • (1995) Acta Crystallog. Sect. D , vol.51 , pp. 220-231
    • Chen, Y.W.1    Fersht, A.R.2    Henrick, K.3
  • 8
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. (1990). Dominant forces in protein folding. Biochemistry, 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 9
    • 0026567907 scopus 로고
    • Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
    • Eriksson, A. E., Baase, W. A., Zhang, X.-J., Heinz, D. W., Blaber, M., Baldwin, E. P. & Matthews, B. W. (1992). Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science, 255, 178-183.
    • (1992) Science , vol.255 , pp. 178-183
    • Eriksson, A.E.1    Baase, W.A.2    Zhang, X.-J.3    Heinz, D.W.4    Blaber, M.5    Baldwin, E.P.6    Matthews, B.W.7
  • 10
    • 0027394606 scopus 로고
    • Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences
    • Eriksson, A. E., Baase, W. A. & Matthews, B. W. (1993). Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. J. Mol. Biol. 229, 747-769.
    • (1993) J. Mol. Biol. , vol.229 , pp. 747-769
    • Eriksson, A.E.1    Baase, W.A.2    Matthews, B.W.3
  • 12
    • 0028216128 scopus 로고
    • The solution structure of the Tyr41 → His mutant of the single-stranded DNA binding protein encoded by gene V of the filamentous bacteriophage M13
    • Folkers, P. J., Nilges, M., Folmer, R. H., Konings, R. N. & Hilbers, C. W. (1994). The solution structure of the Tyr41 → His mutant of the single-stranded DNA binding protein encoded by gene V of the filamentous bacteriophage M13. J. Mol. Biol. 236, 229-246.
    • (1994) J. Mol. Biol. , vol.236 , pp. 229-246
    • Folkers, P.J.1    Nilges, M.2    Folmer, R.H.3    Konings, R.N.4    Hilbers, C.W.5
  • 13
    • 0028066921 scopus 로고
    • A model of the complex between single-stranded DNA and the single-stranded DNA binding protein encoded by gene V of filamentous bacteriophage M13
    • Folmer, R. H., Nilges, M., Folkers, P. J., Konings, R. N. H. & Hilbers, C. W. (1994). A model of the complex between single-stranded DNA and the single-stranded DNA binding protein encoded by gene V of filamentous bacteriophage M13. J. Mol. Biol. 240, 341-357.
    • (1994) J. Mol. Biol. , vol.240 , pp. 341-357
    • Folmer, R.H.1    Nilges, M.2    Folkers, P.J.3    Konings, R.N.H.4    Hilbers, C.W.5
  • 14
    • 0027383834 scopus 로고
    • Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease
    • Green, S. M. & Shortle, D. (1993). Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. Biochemistry, 32, 10131-10139.
    • (1993) Biochemistry , vol.32 , pp. 10131-10139
    • Green, S.M.1    Shortle, D.2
  • 15
    • 0023660935 scopus 로고
    • Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157-Ile
    • Grutter, M. G., Gray T. M., Weaver, L. H., Alber, T., Wilson, K. & Matthews, B. W. (1987). Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157-Ile. J. Mol. Biol. 197, 315-329.
    • (1987) J. Mol. Biol. , vol.197 , pp. 315-329
    • Grutter, M.G.1    Gray, T.M.2    Weaver, L.H.3    Alber, T.4    Wilson, K.5    Matthews, B.W.6
  • 16
    • 0028334576 scopus 로고
    • Crystal structures of Y41H and Y41F mutants of gene V protein from Ff phage suggest possible protein-protein interactions in the GVP-ssDNA complex
    • Guan, Y., Zhang, H., Konings, R. N., Hilbers, C. W., Terwilliger, T. C. & Wang, A. H. (1994). Crystal structures of Y41H and Y41F mutants of gene V protein from Ff phage suggest possible protein-protein interactions in the GVP-ssDNA complex. Biochemistry, 33, 7768-7778.
    • (1994) Biochemistry , vol.33 , pp. 7768-7778
    • Guan, Y.1    Zhang, H.2    Konings, R.N.3    Hilbers, C.W.4    Terwilliger, T.C.5    Wang, A.H.6
  • 17
    • 0028942225 scopus 로고
    • Electrostatic potential distribution of the gene V protein from Ff phage facilitates cooperative DNA binding: A model of the GVP-ssDNA complex
    • Guan, Y., Zhang, H. & Wang, A. H. (1995). Electrostatic potential distribution of the gene V protein from Ff phage facilitates cooperative DNA binding: a model of the GVP-ssDNA complex. Protein Sci. 4735, 187-197.
    • (1995) Protein Sci. , vol.4735 , pp. 187-197
    • Guan, Y.1    Zhang, H.2    Wang, A.H.3
  • 18
    • 0026532266 scopus 로고
    • Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme
    • Hurley, J. H., Baase, W. A. & Matthews, B. W. (1992). Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. J. Mol. Biol. 224, 1143-1159.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1143-1159
    • Hurley, J.H.1    Baase, W.A.2    Matthews, B.W.3
  • 19
    • 0027384577 scopus 로고
    • Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
    • Jackson, S. E., Moracci, M., elMasry N., Johnson, C. M. & Fersht, A. R. (1993). Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry, 32, 11259-11269.
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    ElMasry, N.3    Johnson, C.M.4    Fersht, A.R.5
  • 20
    • 0018115846 scopus 로고
    • Conformation of amino acid side-chains in proteins
    • Janin, J. & Wodak, S. (1978). Conformation of amino acid side-chains in proteins. J. Mol. Biol. 125, 357-386.
    • (1978) J. Mol. Biol. , vol.125 , pp. 357-386
    • Janin, J.1    Wodak, S.2
  • 21
    • 0022333120 scopus 로고
    • Interactive computer graphics: FRODO
    • Jones, T. A. (1985). Interactive computer graphics: FRODO. Methods Enzymol. 115, 157-171.
    • (1985) Methods Enzymol. , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 23
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann, W. (1959). Some factors in the interpretation of protein denaturation. Advan. Protein Chem. 14, 1-63.
    • (1959) Advan. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 24
    • 0024375463 scopus 로고
    • Energetics of complementary side-chain packing in a protein hydrophobic core
    • Kellis, J. T., Jr, Nyberg, K. & Fersht, A. R. (1989). Energetics of complementary side-chain packing in a protein hydrophobic core. Biochemistry, 28, 4914-4922.
    • (1989) Biochemistry , vol.28 , pp. 4914-4922
    • Kellis J.T., Jr.1    Nyberg, K.2    Fersht, A.R.3
  • 25
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility J
    • Lee, B. & Richards, F. M. (1971). The interpretation of protein structures: estimation of static accessibility J. Mol. Biol. 55, 379-400.
    • (1971) Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 26
    • 0025727457 scopus 로고
    • Reversible denaturation of the gene V protein of bacteriophage f1
    • Liang, H. & Terwilliger, T. C. (1991). Reversible denaturation of the gene V protein of bacteriophage f1. Biochemistry, 30, 2772-2782.
    • (1991) Biochemistry , vol.30 , pp. 2772-2782
    • Liang, H.1    Terwilliger, T.C.2
  • 27
    • 0028965496 scopus 로고
    • Long-range, small magnitude nonadditivity of mutational effects in proteins
    • LiCata, V. J. & Ackers, G. K. (1995). Long-range, small magnitude nonadditivity of mutational effects in proteins. Biochemistry, 34, 3133-3139.
    • (1995) Biochemistry , vol.34 , pp. 3133-3139
    • LiCata, V.J.1    Ackers, G.K.2
  • 28
    • 0024507791 scopus 로고
    • Alternative packing arrangements in the hydrophobic core of lambda repressor
    • Lim, W. A. & Sauer, R. T. (1989). Alternative packing arrangements in the hydrophobic core of lambda repressor. Nature, 339, 31-36.
    • (1989) Nature , vol.339 , pp. 31-36
    • Lim, W.A.1    Sauer, R.T.2
  • 29
    • 0026766573 scopus 로고
    • Structural and energetic consequences of disruptive mutations in a protein core
    • Lim, W. A., Farruggio, D. C. & Sauer, R. T. (1992). Structural and energetic consequences of disruptive mutations in a protein core. Biochemistry, 31, 4324-4333.
    • (1992) Biochemistry , vol.31 , pp. 4324-4333
    • Lim, W.A.1    Farruggio, D.C.2    Sauer, R.T.3
  • 30
    • 0023741058 scopus 로고
    • Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile3
    • Matsumura, M., Becktel, W. J. & Matthews, B. W. (1988). Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile3. Nature, 334, 406-410.
    • (1988) Nature , vol.334 , pp. 406-410
    • Matsumura, M.1    Becktel, W.J.2    Matthews, B.W.3
  • 31
    • 0023643422 scopus 로고
    • Genetics and structural analysis of the protein stability problem
    • Matthews, B. W. (1987). Genetics and structural analysis of the protein stability problem. Biochemistry, 26, 6885-6888.
    • (1987) Biochemistry , vol.26 , pp. 6885-6888
    • Matthews, B.W.1
  • 32
    • 0017202841 scopus 로고
    • Crystallization of a DNA unwinding protein: Preliminary X-ray analysis of fd bacteriophage gene 5 product
    • McPherson, A., Molineux, I. & Rich, A. (1976). Crystallization of a DNA unwinding protein: preliminary X-ray analysis of fd bacteriophage gene 5 product. J. Mol. Biol. 106, 1077-1081.
    • (1976) J. Mol. Biol. , vol.106 , pp. 1077-1081
    • McPherson, A.1    Molineux, I.2    Rich, A.3
  • 33
    • 0029017513 scopus 로고
    • Structures of fd gene 5 protein nucleic acid complexes: A combined solution scattering and electron microscopy study
    • Olah, G. A., Gray, D. M., Gray, C. W., Kergil, D. L., Sosnick, T. R., Mark, B. L., Vaughan, R. & Trewhella, J. (1995). Structures of fd gene 5 protein nucleic acid complexes: a combined solution scattering and electron microscopy study J. Mol. Biol. 249, 576-594.
    • (1995) J. Mol. Biol. , vol.249 , pp. 576-594
    • Olah, G.A.1    Gray, D.M.2    Gray, C.W.3    Kergil, D.L.4    Sosnick, T.R.5    Mark, B.L.6    Vaughan, R.7    Trewhella, J.8
  • 34
    • 0026777217 scopus 로고
    • Contribution of the hydrophobic effect to globular protein stability
    • Pace, C. N. (1992). Contribution of the hydrophobic effect to globular protein stability J. Mol. Biol. 226, 29-35.
    • (1992) J. Mol. Biol. , vol.226 , pp. 29-35
    • Pace, C.N.1
  • 35
    • 0023155210 scopus 로고
    • Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder, J. W. & Richards, F. M. (1987). Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193, 775-791.
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 36
    • 0015977588 scopus 로고
    • The interpretation of protein structures: Total volume, group volume distributions and packing density
    • Richards, F. M. (1974). The interpretation of protein structures: total volume, group volume distributions and packing density J. Mol. Biol. 82, 1-14.
    • (1974) J. Mol. Biol. , vol.82 , pp. 1-14
    • Richards, F.M.1
  • 37
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards, F. M. (1977). Areas, volumes, packing and protein structure. Annu. Rev. Biophys. Bioeng. 6, 151-176.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 38
    • 0024400292 scopus 로고
    • Influence of interior packing and hydrophobicity on the stability of a protein
    • Sandberg, W. S. & Terwilliger, T. C. (1989). Influence of interior packing and hydrophobicity on the stability of a protein. Science, 245, 54-57.
    • (1989) Science , vol.245 , pp. 54-57
    • Sandberg, W.S.1    Terwilliger, T.C.2
  • 41
    • 0027248706 scopus 로고
    • Engineering multiple properties of a protein by combinatorial mutagenesis
    • Sandberg, W. S. & Terwillinger, T. C. (1993). Engineering multiple properties of a protein by combinatorial mutagenesis. Proc. Natl Acad. Sci. USA, 90, 8367-8371.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8367-8371
    • Sandberg, W.S.1    Terwillinger, T.C.2
  • 42
    • 0026553768 scopus 로고
    • The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability
    • Serrano, L., Kellis, J. T., Jr, Cann, P., Matouschek, A. & Fersht A. T. (1992). The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability J. Mol. Biol. 224, 783-804.
    • (1992) J. Mol. Biol. , vol.224 , pp. 783-804
    • Serrano, L.1    Kellis J.T., Jr.2    Cann, P.3    Matouschek, A.4    Fersht, A.T.5
  • 43
    • 0025005525 scopus 로고
    • Contribution of the large hydrophobic amino acids to the stability of staphylococcal nuclease
    • Shortle, D. Stites, W. E. & Meeker, A. K. (1990). Contribution of the large hydrophobic amino acids to the stability of staphylococcal nuclease. Biochemistry, 29, 8033-8041.
    • (1990) Biochemistry , vol.29 , pp. 8033-8041
    • Shortle, D.1    Stites, W.E.2    Meeker, A.K.3
  • 45
    • 0026566303 scopus 로고
    • The role of packing interactions in stabilizing folded proteins
    • Sneddon, S. F. & Tobias, D. J. (1992). The role of packing interactions in stabilizing folded proteins. Biochemistry, 31, 2842-2846.
    • (1992) Biochemistry , vol.31 , pp. 2842-2846
    • Sneddon, S.F.1    Tobias, D.J.2
  • 46
    • 0028174101 scopus 로고
    • Protein side-chain conformational entropy derived from fusion data-comparison with other empirical scales
    • Sternberg, M. J. & Chickos, J. S. (1994). Protein side-chain conformational entropy derived from fusion data-comparison with other empirical scales. Protein Eng. 7, 149-155.
    • (1994) Protein Eng. , vol.7 , pp. 149-155
    • Sternberg, M.J.1    Chickos, J.S.2
  • 48
    • 0028801485 scopus 로고
    • Difference refinement: Obtaining differences between two related structures
    • Terwilliger, T. C. & Berendzen, J. (1995). Difference refinement: obtaining differences between two related structures. Acta Crystallog. sect. D, 51, 609-618.
    • (1995) Acta Crystallog. Sect. D , vol.51 , pp. 609-618
    • Terwilliger, T.C.1    Berendzen, J.2
  • 49
    • 0026998178 scopus 로고
    • Crystallographic structures of ribonuclease S variants with nonpolar substitutions at position 13: Packing and cavities
    • Varadarajan, R. & Richards, F. M. (1992). Crystallographic structures of ribonuclease S variants with nonpolar substitutions at position 13: packing and cavities. Biochemistry, 31, 12315-12327.
    • (1992) Biochemistry , vol.31 , pp. 12315-12327
    • Varadarajan, R.1    Richards, F.M.2
  • 50
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells, J. A. (1990). Additivity of mutational effects in proteins. Biochemistry, 29, 8509-8517.
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1
  • 51
    • 0026757625 scopus 로고
    • Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme
    • Wilson, K. P. B., Malcolm, A. & Matthews, B. W. (1992). Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme. J. Biol. Chem. 267, 10842-10849.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10842-10849
    • Wilson, K.P.B.1    Malcolm, A.2    Matthews, B.W.3
  • 52
    • 0025875188 scopus 로고
    • Isolation and in vitro characterization of temperature sensitive mutants of the bacteriophage f1 gene V protein
    • Zabin, H. B. & Terwilliger T. C. (1991). Isolation and in vitro characterization of temperature sensitive mutants of the bacteriophage f1 gene V protein. J. Mol. Biol. 219, 257-275.
    • (1991) J. Mol. Biol. , vol.219 , pp. 257-275
    • Zabin, H.B.1    Terwilliger, T.C.2


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