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Volumn 326, Issue 1, 2003, Pages 293-305

Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: Similarities and differences in the folding of homologous proteins

Author keywords

Folding; Immunity protein; Topology; Transition state; value

Indexed keywords

BACTERIAL PROTEIN; IMMUNITY PROTEIN 7; IMMUNITY PROTEIN 9; UNCLASSIFIED DRUG;

EID: 0037423705     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01249-4     Document Type: Article
Times cited : (128)

References (36)
  • 1
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker D. A surprising simplicity to protein folding. Nature. 405:2000;39-42.
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 2
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco K.W., Simons K.T., Baker D. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277:1998;985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 3
    • 0032750509 scopus 로고    scopus 로고
    • The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
    • Martinez J.C., Serrano L. The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nature Struct. Biol. 6:1999;1010-1016.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 1010-1016
    • Martinez, J.C.1    Serrano, L.2
  • 5
    • 0036172116 scopus 로고    scopus 로고
    • Hydrophobic core packing in the SH3 domain folding transition state
    • Northey J.G.B., Di Nardo A.A., Davidson A.R. Hydrophobic core packing in the SH3 domain folding transition state. Nature Struct. Biol. 9:2002;126-130.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 126-130
    • Northey, J.G.B.1    Di Nardo, A.A.2    Davidson, A.R.3
  • 7
    • 0032515105 scopus 로고    scopus 로고
    • Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain
    • Villegas V., Martinez J.C., Aviles F.X., Serrano L. Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283:1998;1027-1036.
    • (1998) J. Mol. Biol. , vol.283 , pp. 1027-1036
    • Villegas, V.1    Martinez, J.C.2    Aviles, F.X.3    Serrano, L.4
  • 9
    • 0033871567 scopus 로고    scopus 로고
    • Critical role of β-hairpin formation in protein G folding
    • McCallister E.L., Alm E., Baker D. Critical role of β-hairpin formation in protein G folding. Nature Struct. Biol. 7:2000;669-673.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 669-673
    • McCallister, E.L.1    Alm, E.2    Baker, D.3
  • 10
    • 0034964196 scopus 로고    scopus 로고
    • Computer-based redesign of a protein folding pathway
    • Nauli S., Kuhlman B., Baker D. Computer-based redesign of a protein folding pathway. Nature Struct. Biol. 8:2001;602-605.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 602-605
    • Nauli, S.1    Kuhlman, B.2    Baker, D.3
  • 11
    • 0036300662 scopus 로고    scopus 로고
    • Accurate computer-based design of a new backbone conformation in the second turn of protein L
    • Kuhlman B., O'Neill J.W., Kim D.E., Zhang K.Y.L., Baker D. Accurate computer-based design of a new backbone conformation in the second turn of protein L. J. Mol. Biol. 315:2002;471-477.
    • (2002) J. Mol. Biol. , vol.315 , pp. 471-477
    • Kuhlman, B.1    O'Neill, J.W.2    Kim, D.E.3    Zhang, K.Y.L.4    Baker, D.5
  • 13
    • 0032554626 scopus 로고    scopus 로고
    • Protein folding dynamics: Quantitative comparison between theory and experiment
    • Burton R.E., Myers J.K., Oas T.G. Protein folding dynamics: quantitative comparison between theory and experiment. Biochemistry. 37:1998;5337-5343.
    • (1998) Biochemistry , vol.37 , pp. 5337-5343
    • Burton, R.E.1    Myers, J.K.2    Oas, T.G.3
  • 14
    • 0035324637 scopus 로고    scopus 로고
    • How Ala-Gly mutations in different helices affect the stability of the apomyoglobin molten globule
    • Luo Y., Baldwin R.L. How Ala-Gly mutations in different helices affect the stability of the apomyoglobin molten globule. Biochemistry. 40:2001;5283-5289.
    • (2001) Biochemistry , vol.40 , pp. 5283-5289
    • Luo, Y.1    Baldwin, R.L.2
  • 15
    • 0036307683 scopus 로고    scopus 로고
    • Application of the diffusion-collision model to the folding of three-helix bundle proteins
    • Islam S.A., Karplus M., Weaver D.L. Application of the diffusion-collision model to the folding of three-helix bundle proteins. J. Mol. Biol. 318:2002;199-215.
    • (2002) J. Mol. Biol. , vol.318 , pp. 199-215
    • Islam, S.A.1    Karplus, M.2    Weaver, D.L.3
  • 17
    • 0036183221 scopus 로고    scopus 로고
    • Im7 folding mechanism: Misfolding on a path to the native state
    • Capaldi A.P., Kleanthous C., Radford S.E. Im7 folding mechanism: misfolding on a path to the native state. Nature Struct. Biol. 9:2002;209-216.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 209-216
    • Capaldi, A.P.1    Kleanthous, C.2    Radford, S.E.3
  • 18
    • 0033548553 scopus 로고    scopus 로고
    • Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9
    • Ferguson N., Capaldi A.P., James R., Kleanthous C., Radford S.E. Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9. J. Mol. Biol. 286:1999;1597-1608.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1597-1608
    • Ferguson, N.1    Capaldi, A.P.2    James, R.3    Kleanthous, C.4    Radford, S.E.5
  • 19
    • 0035896036 scopus 로고    scopus 로고
    • Using chimeric immunity proteins to explore the energy landscape for α-helical protein folding
    • Ferguson N., Li W., Capaldi A.P., Kleanthous C., Radford S.E. Using chimeric immunity proteins to explore the energy landscape for α-helical protein folding. J. Mol. Biol. 307:2001;393-405.
    • (2001) J. Mol. Biol. , vol.307 , pp. 393-405
    • Ferguson, N.1    Li, W.2    Capaldi, A.P.3    Kleanthous, C.4    Radford, S.E.5
  • 20
    • 0035965128 scopus 로고    scopus 로고
    • Acidic conditions stabilise imtermediates populated during the folding of Im7 and Im9
    • Gorski S.A., Capaldi A.P., Kleanthous C., Radford S.E. Acidic conditions stabilise imtermediates populated during the folding of Im7 and Im9. J. Mol. Biol. 312:2001;849-863.
    • (2001) J. Mol. Biol. , vol.312 , pp. 849-863
    • Gorski, S.A.1    Capaldi, A.P.2    Kleanthous, C.3    Radford, S.E.4
  • 21
    • 0035478958 scopus 로고    scopus 로고
    • Immunity proteins: Enzyme inhibitors that avoid the active site
    • Kleanthous C., Walker D. Immunity proteins: enzyme inhibitors that avoid the active site. Trends Biochem. Sci. 26:2001;624-631.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 624-631
    • Kleanthous, C.1    Walker, D.2
  • 22
    • 0026511656 scopus 로고
    • The folding of an enzyme. 1. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht A.R., Matouschek A., Serrano L. The folding of an enzyme. 1. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224:1992;771-782.
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 24
    • 0030867940 scopus 로고    scopus 로고
    • Protein-protein interaction specificity of Im9 for the endonuclease toxin colicin E9 defined by homologue-scanning mutagenesis
    • Li W., Dennis C.A., Moore G.R., James R., Kleanthous C. Protein-protein interaction specificity of Im9 for the endonuclease toxin colicin E9 defined by homologue-scanning mutagenesis. J. Biol. Chem. 272:1997;22253-22258.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22253-22258
    • Li, W.1    Dennis, C.A.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 25
    • 0032566286 scopus 로고    scopus 로고
    • Dual recognition and the role of specificity-determining residues in colicin E9 DNase-immunity protein interactions
    • Li W., Hammil S.J., Hemmings A.M., Moore G.R., James R., Kleanthous C. Dual recognition and the role of specificity-determining residues in colicin E9 DNase-immunity protein interactions. Biochemistry. 37:1998;11771-11779.
    • (1998) Biochemistry , vol.37 , pp. 11771-11779
    • Li, W.1    Hammil, S.J.2    Hemmings, A.M.3    Moore, G.R.4    James, R.5    Kleanthous, C.6
  • 26
    • 0034283147 scopus 로고    scopus 로고
    • Specificity in protein-protein interactions: The structural basis for dual recognition in endonuclease colicin-immunity protein complexes
    • Kulmann U.C., Pommer A.J., Moore G.R., James R., Kleanthous C. Specificity in protein-protein interactions: the structural basis for dual recognition in endonuclease colicin-immunity protein complexes. J. Mol. Biol. 301:2000;1163-1178.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1163-1178
    • Kulmann, U.C.1    Pommer, A.J.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 27
    • 0032512424 scopus 로고    scopus 로고
    • Specificity in protein-protein recognition: Conserved Im9 residues are the major determinants of stability in the colicin E9 DNase-Im9 complex
    • Wallis R., Leung K.-Y., Osbourne M.J., James R., Moore G., Kleanthous C. Specificity in protein-protein recognition: conserved Im9 residues are the major determinants of stability in the colicin E9 DNase-Im9 complex. Biochemistry. 37:1998;476-485.
    • (1998) Biochemistry , vol.37 , pp. 476-485
    • Wallis, R.1    Leung, K.-Y.2    Osbourne, M.J.3    James, R.4    Moore, G.5    Kleanthous, C.6
  • 28
    • 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. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 29
    • 0032553332 scopus 로고    scopus 로고
    • Elucidating the folding problem of α-helices: Local motifs, long-range electrostatics, ionic strength dependence and prediction of NMR parameters
    • Lacroix E., Viguera A.R., Serrano L. Elucidating the folding problem of α-helices: local motifs, long-range electrostatics, ionic strength dependence and prediction of NMR parameters. J. Mol. Biol. 284:1998;173-191.
    • (1998) J. Mol. Biol. , vol.284 , pp. 173-191
    • Lacroix, E.1    Viguera, A.R.2    Serrano, L.3
  • 30
    • 0028873081 scopus 로고
    • Elucidating the folding problem of α-helical peptides using empirical parameters. II. Helix macrodiapole effects and rational modification of the helical content of natural peptides
    • Muñoz V., Serrano L. Elucidating the folding problem of α-helical peptides using empirical parameters. II. Helix macrodiapole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 245:1994;275-296.
    • (1994) J. Mol. Biol. , vol.245 , pp. 275-296
    • Muñoz, V.1    Serrano, L.2
  • 31
    • 0028834210 scopus 로고
    • Elucidating the folding problem of α-helical peptides using empirical parameters. III. Temperature and pH dependence
    • Muñoz V., Serrano L. Elucidating the folding problem of α-helical peptides using empirical parameters. III. Temperature and pH dependence. J. Mol. Biol. 245:1994;297-308.
    • (1994) J. Mol. Biol. , vol.245 , pp. 297-308
    • Muñoz, V.1    Serrano, L.2
  • 32
    • 0031127043 scopus 로고    scopus 로고
    • Development of multiple sequence approximation within the Agadir model of α-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Muñoz V., Serrano L. Development of multiple sequence approximation within the Agadir model of α-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers. 41:1997;495-509.
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Muñoz, V.1    Serrano, L.2
  • 33
    • 0033592876 scopus 로고    scopus 로고
    • From snapshot to movie: Φ analysis of protein folding transition states taken one step further
    • Ternstom T., Mayor U., Akke M., Oliveberg M. From snapshot to movie: Φ analysis of protein folding transition states taken one step further. Proc. Natl Acad. Sci. USA. 96:1999;14854-14859.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 14854-14859
    • Ternstom, T.1    Mayor, U.2    Akke, M.3    Oliveberg, M.4
  • 34
    • 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. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 35
    • 0030815133 scopus 로고    scopus 로고
    • Raster 3D: Photorealistic molecular graphics
    • Merrit E.A., Bacon D.J. Raster 3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2
  • 36
    • 0032127769 scopus 로고    scopus 로고
    • A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificity
    • Dennis C.A., Videler H., Paupit R.A., Wallis R., James R., Moore G.R., Kleanthous C. A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificity. Biochem. J. 333:1998;183-191.
    • (1998) Biochem. J. , vol.333 , pp. 183-191
    • Dennis, C.A.1    Videler, H.2    Paupit, R.A.3    Wallis, R.4    James, R.5    Moore, G.R.6    Kleanthous, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.