메뉴 건너뛰기




Volumn 44, Issue 34, 2005, Pages 11496-11507

Clusters in an intrinsically disordered protein create a protein-binding site: The TolB-binding region of colicin E9

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DNA; MUTAGENESIS; POLYPEPTIDES; TOXIC MATERIALS;

EID: 23944444257     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0503596     Document Type: Article
Times cited : (25)

References (61)
  • 1
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E., and Dyson, H. J. (1999) Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm, J. Mol. Biol 293, 321-331.
    • (1999) J. Mol. Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 3
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. (2002) Natively unfolded proteins: A point where biology waits for physics, Protein Sci. 11, 739-756.
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 4
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J., and Wright, P. E. (2002) Coupling of folding and binding for unstructured proteins, Curr. Opin. Struct. Biol. 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 5
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R. S., and Record, M. T. (1994) Coupling of local folding to site-specific binding of proteins to DNA, Science 263, 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, M.T.2
  • 6
    • 0027311259 scopus 로고
    • Close encounters: Why unstructured, polymeric domains can increase rates of specific macromolecular association
    • Pontius, B. W. (1993) Close encounters: Why unstructured, polymeric domains can increase rates of specific macromolecular association, Trends Biochem. Sci. 18, 181-186.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 181-186
    • Pontius, B.W.1
  • 7
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker, B. A., Portman, J. J., and Wolynes, P. G. (2000) Speeding molecular recognition by using the folding funnel: The fly-casting mechanism. Proc. Natl. Acad. Sci. U.S.A. 97, 8868-8873.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 8
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21Wal1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity
    • Kriwacki, R. W., Hengst, L., Tennant, L., Reed, S. I., and Wright, P. E. (1996) Structural studies of p21Wal1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity, Proc. Natl. Acad. Sci. U.S.A. 93, 11504-11509.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5
  • 13
    • 0036589253 scopus 로고    scopus 로고
    • Killing of E. coli cells by e group nuclease colicins
    • James, R., Penfold, C. N., Moore, G. R., and Kleanthous, C. (2002) Killing of E. coli cells by E group nuclease colicins, Biochimie 84, 381-389.
    • (2002) Biochimie , vol.84 , pp. 381-389
    • James, R.1    Penfold, C.N.2    Moore, G.R.3    Kleanthous, C.4
  • 14
    • 0037064252 scopus 로고    scopus 로고
    • Colicin crystal structures: Pathways and mechanisms for colicin insertion into membranes
    • Zakharov, S. D., and Cramer, W. A. (2002) Colicin crystal structures: Pathways and mechanisms for colicin insertion into membranes, Biochim. Biophys. Acta 1565, 333-346.
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 333-346
    • Zakharov, S.D.1    Cramer, W.A.2
  • 16
    • 0036589207 scopus 로고    scopus 로고
    • Mechanisms of colicin binding and transport through outer membrane porins
    • Cao, Z., and Klebba, P. E. (2002) Mechanisms of colicin binding and transport through outer membrane porins, Biochimie 84, 399-412.
    • (2002) Biochimie , vol.84 , pp. 399-412
    • Cao, Z.1    Klebba, P.E.2
  • 17
    • 0028905676 scopus 로고
    • Novel colicin 10: Assignment of four domains to TonB- and TolC-dependent uptake via the Tsx receptor and to pore formation
    • Pilsl, H., and Braun, V. (1995) Novel colicin 10: Assignment of four domains to TonB- and TolC-dependent uptake via the Tsx receptor and to pore formation, Mol. Microbiol. 16, 57-67.
    • (1995) Mol. Microbiol. , vol.16 , pp. 57-67
    • Pilsl, H.1    Braun, V.2
  • 18
    • 0030754709 scopus 로고    scopus 로고
    • Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9
    • Garinot-Schneider, C., Penfold, C. N., Moore, G. R., Kleanthous, C., and James, R. (1997) Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9, Microbiology 143, 2931-2938.
    • (1997) Microbiology , vol.143 , pp. 2931-2938
    • Garinot-Schneider, C.1    Penfold, C.N.2    Moore, G.R.3    Kleanthous, C.4    James, R.5
  • 19
    • 0031983893 scopus 로고    scopus 로고
    • Distinct regions of the colicin a translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli
    • Bouveret, E., Rigal, A., Lazdunski, C., and Bénédetti, H. (1998) Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli, Mol. Microbiol. 27, 143-157.
    • (1998) Mol. Microbiol. , vol.27 , pp. 143-157
    • Bouveret, E.1    Rigal, A.2    Lazdunski, C.3    Bénédetti, H.4
  • 20
    • 0034650563 scopus 로고    scopus 로고
    • The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9
    • Carr, S., Penfold, C. N., Bamford, V., James, R., and Hemmings, A. M. (2000) The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9, Structure 8, 57-66.
    • (2000) Structure , vol.8 , pp. 57-66
    • Carr, S.1    Penfold, C.N.2    Bamford, V.3    James, R.4    Hemmings, A.M.5
  • 22
    • 0033569296 scopus 로고    scopus 로고
    • Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 Å resolution
    • Abergel, C., Bouveret, E., Claverie, J.-M., Brown, K., Rigal, A., Lazdunski, C., and Bénédetti, H. (1999) Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 Å resolution, Structure 7, 1291-1300.
    • (1999) Structure , vol.7 , pp. 1291-1300
    • Abergel, C.1    Bouveret, E.2    Claverie, J.-M.3    Brown, K.4    Rigal, A.5    Lazdunski, C.6    Bénédetti, H.7
  • 23
    • 0035930345 scopus 로고    scopus 로고
    • Crystal structure of colicin E3: Implications for cell entry and ribosome inactivation
    • Soelaiman, S., Jakes, K., Wu, N., Li, C., and Shoham, M. (2001) Crystal structure of colicin E3: Implications for cell entry and ribosome inactivation, Mol. Cell 8, 1053-1062.
    • (2001) Mol. Cell , vol.8 , pp. 1053-1062
    • Soelaiman, S.1    Jakes, K.2    Wu, N.3    Li, C.4    Shoham, M.5
  • 26
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 28
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T. H., Billeter, M., Güntert, P., and Wüthrich, K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J Biomol. NMR 6, 1-10.
    • (1995) J Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 31
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel A., M., Akke, M., and Palmer, A. G., III (1995) Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme, J. Mol. Biol 246, 144-163.
    • (1995) J. Mol. Biol , vol.246 , pp. 144-163
    • Mandel, A.1    Akke, M.2    Palmer III, A.G.3
  • 32
  • 34
    • 0025904730 scopus 로고
    • Defining solution conformations of small linear peptides
    • Dyson, H. J., and Wright, P. E. (1991) Defining solution conformations of small linear peptides, Annu. Rev. Biophys. Biophys. Chem. 20, 519-538.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 519-538
    • Dyson, H.J.1    Wright, P.E.2
  • 35
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease, Biochemistry 28, 8972-8979.
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 36
    • 0037159208 scopus 로고    scopus 로고
    • Molecular hinges in protein folding: The urea-denatured state of apomyoglobin
    • Schwarzinger, S., Wright, P. E., and Dyson, H. J. (2002) Molecular hinges in protein folding: The urea-denatured state of apomyoglobin, Biochemistry 41, 12681-12686.
    • (2002) Biochemistry , vol.41 , pp. 12681-12686
    • Schwarzinger, S.1    Wright, P.E.2    Dyson, H.J.3
  • 37
    • 0035957221 scopus 로고    scopus 로고
    • NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin: A model system for the initial steps of folding
    • Yao, J., Chung, J., Eliezer, D., Wright, P. E., and Dyson, H. J. (2001) NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin: A model system for the initial steps of folding, Biochemistry 40, 3561-3571.
    • (2001) Biochemistry , vol.40 , pp. 3561-3571
    • Yao, J.1    Chung, J.2    Eliezer, D.3    Wright, P.E.4    Dyson, H.J.5
  • 39
    • 0026784152 scopus 로고
    • Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments
    • Peng, J. W., and Wagner, G. (1992) Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments, Biochemistry 31, 8571-8586.
    • (1992) Biochemistry , vol.31 , pp. 8571-8586
    • Peng, J.W.1    Wagner, G.2
  • 41
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • Palmer, A. G., III (2004) NMR characterization of the dynamics of biomacromolecules, Chem. Rev. 104, 3623-3640.
    • (2004) Chem. Rev. , vol.104 , pp. 3623-3640
    • Palmer III, A.G.1
  • 42
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson, H. J., and Wright, P. E. (2004) Unfolded proteins and protein folding studied by NMR, Chem. Rev. 104, 3607-3622.
    • (2004) Chem. Rev. , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 43
    • 0030759665 scopus 로고    scopus 로고
    • Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea
    • Schwalbe, H., Fiebig, K. M., Buck, M., Jones, J. A., Grimshaw, S. B., Spencer, A., Glaser, S. J., Smith, L. J., and Dobson, C. M. (1997) Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea, Biochemistry 36, 8977-8991.
    • (1997) Biochemistry , vol.36 , pp. 8977-8991
    • Schwalbe, H.1    Fiebig, K.M.2    Buck, M.3    Jones, J.A.4    Grimshaw, S.B.5    Spencer, A.6    Glaser, S.J.7    Smith, L.J.8    Dobson, C.M.9
  • 44
    • 0020475449 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Kyte, J., and Doolittle, B. F. (1982) Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences, J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, B.F.2
  • 45
    • 0023657949 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Gaboriaud, C., Bissery, V., Benchetrit, T., and Mornon, J.-P. (1987) A simple method for displaying the hydropathic character of a protein, FEBS Lett. 224, 149-155.
    • (1987) FEBS Lett. , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.-P.4
  • 46
    • 0022412192 scopus 로고
    • Hydrophobicity of amino acid residues in globular proteins
    • Rose, G. D., Geselowitz, A. R., Lesser, G. J., Lee, R. H., and Zehfus, M. H. (1985) Hydrophobicity of amino acid residues in globular proteins, Science 229, 834-838.
    • (1985) Science , vol.229 , pp. 834-838
    • Rose, G.D.1    Geselowitz, A.R.2    Lesser, G.J.3    Lee, R.H.4    Zehfus, M.H.5
  • 48
    • 0032900496 scopus 로고    scopus 로고
    • Prediction of the location and type of β-turns in proteins using neural networks
    • Shepherd, A. J., Corse, D., and Thornton, J. M. (1999) Prediction of the location and type of β-turns in proteins using neural networks, Protein Sci. 8, 1045-1055.
    • (1999) Protein Sci. , vol.8 , pp. 1045-1055
    • Shepherd, A.J.1    Corse, D.2    Thornton, J.M.3
  • 49
    • 1242273667 scopus 로고    scopus 로고
    • The structure and mechanism of methanol dehydrogenase
    • Anthony, C., and Williams, P. (2003) The structure and mechanism of methanol dehydrogenase, Biochim. Biophys. Acta 1647, 18-25.
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 18-25
    • Anthony, C.1    Williams, P.2
  • 50
    • 0029643953 scopus 로고
    • The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 Å
    • Ghosh, M., Anthony, C., Harlos, K., Goodwin, M. G., and Blake, C. C. F. (1995) The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 Å, Structure 3, 177-187.
    • (1995) Structure , vol.3 , pp. 177-187
    • Ghosh, M.1    Anthony, C.2    Harlos, K.3    Goodwin, M.G.4    Blake, C.C.F.5
  • 51
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter, M., Simon, I., Friedrich, P., and Tompa, P. (2004) Preformed structural elements feature in partner recognition by intrinsically unstructured proteins, J. Mol. Biol. 338, 1015-1026.
    • (2004) J. Mol. Biol. , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 53
  • 55
    • 0000332920 scopus 로고    scopus 로고
    • Sequence data analysis for long disordered regions prediction in the calcineurin family
    • Romero, P., Obradovic, Z., and Dunker, A. K. (1997) Sequence data analysis for long disordered regions prediction in the calcineurin family, Genome Informatics 8, 110-124.
    • (1997) Genome Informatics , vol.8 , pp. 110-124
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 57
    • 1242297815 scopus 로고    scopus 로고
    • Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 Å resolution
    • Hilsenbeck, J. L., Park, H., Chen, G., Youn, B., Postle, K., and Kang, C. (2003) Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 Å resolution, Mol. Microbiol. 51, 711-720.
    • (2003) Mol. Microbiol. , vol.51 , pp. 711-720
    • Hilsenbeck, J.L.1    Park, H.2    Chen, G.3    Youn, B.4    Postle, K.5    Kang, C.6
  • 59
    • 0037484227 scopus 로고    scopus 로고
    • Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA
    • Anderluh, G., Hong, Q., Boetzel, R., MacDonald, C., Moore, G. R., Virden, R., and Lakey, J. H. (2003) Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA, J. Biol. Chem. 278, 21860-21868.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21860-21868
    • Anderluh, G.1    Hong, Q.2    Boetzel, R.3    MacDonald, C.4    Moore, G.R.5    Virden, R.6    Lakey, J.H.7
  • 60
    • 0034767924 scopus 로고    scopus 로고
    • Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm
    • Journet, L., Bouveret, E., Rigal, A., Lloubes, R., Lazdunski, C., and Bénédetti, H. (2001) Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm, Mol. Microbiol. 42, 331-344.
    • (2001) Mol. Microbiol. , vol.42 , pp. 331-344
    • Journet, L.1    Bouveret, E.2    Rigal, A.3    Lloubes, R.4    Lazdunski, C.5    Bénédetti, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.