메뉴 건너뛰기




Volumn 46, Issue 23, 2007, Pages 6733-6743

Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation

Author keywords

[No Author keywords available]

Indexed keywords

BINDING DOMAIN; MYCOBACTERIUM TUBERCULOSIS; POSITIONING HELIX;

EID: 34250177264     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602546q     Document Type: Article
Times cited : (75)

References (60)
  • 1
    • 0001792698 scopus 로고
    • Hoch, J. A, and Silhavy, T. J, Eds, American Society for Microbiology Press, Washington, D.C
    • Hoch, J. A., and Silhavy, T. J., Eds. (1995) Two-Component Signal Transduction, pp 488, American Society for Microbiology Press, Washington, D.C.
    • (1995) Two-Component Signal Transduction , pp. 488
  • 3
    • 10044252242 scopus 로고    scopus 로고
    • Making sense of it all: Bacterial chemotaxis
    • Wadhams, G. H., and Armitage, J. P. (2004) Making sense of it all: bacterial chemotaxis, Nat. Rev. Mol. Cell Biol. 5, 1024-1037.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 1024-1037
    • Wadhams, G.H.1    Armitage, J.P.2
  • 4
    • 33645881935 scopus 로고    scopus 로고
    • Regulation of bacterial virulence by two-component systems
    • Beier, D., and Gross, R. (2006) Regulation of bacterial virulence by two-component systems, Curr. Opin. Microbiol. 9, 143-152.
    • (2006) Curr. Opin. Microbiol , vol.9 , pp. 143-152
    • Beier, D.1    Gross, R.2
  • 5
    • 27744450676 scopus 로고    scopus 로고
    • Escherichia coli starvation diets: Essential nutrients weigh in distinctly
    • Peterson, C. N., Mandel, M. J., and Silhavy, T. J. (2005) Escherichia coli starvation diets: essential nutrients weigh in distinctly, J. Bacteriol. 187, 7549-7553.
    • (2005) J. Bacteriol , vol.187 , pp. 7549-7553
    • Peterson, C.N.1    Mandel, M.J.2    Silhavy, T.J.3
  • 7
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock, J. B., Ninfa, A. J., and Stock, A. M. (1989) Protein phosphorylation and regulation of adaptive responses in bacteria, Microbiol. Rev. 53, 450-490.
    • (1989) Microbiol. Rev , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 8
    • 33744983969 scopus 로고    scopus 로고
    • Structural classification of bacterial response regulators: Diversity of output domains and domain combinations
    • Galperin, M. Y. (2006) Structural classification of bacterial response regulators: diversity of output domains and domain combinations, J. Bacteriol. 188, 4169-4182.
    • (2006) J. Bacteriol , vol.188 , pp. 4169-4182
    • Galperin, M.Y.1
  • 9
    • 0031566431 scopus 로고    scopus 로고
    • Structural relationships in the OmpR family of winged-helix transcription factors
    • Martinez-Hackert, E., and Stock, A. M. (1997) Structural relationships in the OmpR family of winged-helix transcription factors, J. Mol. Biol. 269, 301-312.
    • (1997) J. Mol. Biol , vol.269 , pp. 301-312
    • Martinez-Hackert, E.1    Stock, A.M.2
  • 10
    • 0024670936 scopus 로고
    • A bacterial environmental sensor that functions as a protein kinase and stimulates transcriptional activation
    • Igo, M. M., Ninfa, A. J., and Silhavy, T. J. (1989) A bacterial environmental sensor that functions as a protein kinase and stimulates transcriptional activation, Genes Dev. 3, 598-605.
    • (1989) Genes Dev , vol.3 , pp. 598-605
    • Igo, M.M.1    Ninfa, A.J.2    Silhavy, T.J.3
  • 11
    • 0024811077 scopus 로고
    • Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins
    • Makino, K., Shinagawa, H., Amemura, M., Kawamoto, T., Yamada, M., and Nakata, A. (1989) Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins, J. Mol. Biol. 210, 551-559.
    • (1989) J. Mol. Biol , vol.210 , pp. 551-559
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Kawamoto, T.4    Yamada, M.5    Nakata, A.6
  • 12
    • 0029164694 scopus 로고
    • A common switch in activation of the response regulators NtrC and PhoB: Phosphorylation induces dimerization of the receiver modules
    • Fiedler, U., and Weiss, V. (1995) A common switch in activation of the response regulators NtrC and PhoB: phosphorylation induces dimerization of the receiver modules, EMBO J. 14, 3696-3705.
    • (1995) EMBO J , vol.14 , pp. 3696-3705
    • Fiedler, U.1    Weiss, V.2
  • 13
    • 0029896773 scopus 로고    scopus 로고
    • The activation of PhoB by acetylphosphate
    • McCleary, W. R. (1996) The activation of PhoB by acetylphosphate, Mol. Microbiol. 20, 1155-1163.
    • (1996) Mol. Microbiol , vol.20 , pp. 1155-1163
    • McCleary, W.R.1
  • 14
    • 0035798619 scopus 로고    scopus 로고
    • Multimerization of phosphorylated and non-phosphorylated ArcA is necessary for the response regulator function of the Arc two-component signal transduction system
    • Jeon, Y., Lee, Y. S., Han, J. S., Kim, J. B., and Hwang, D. S. (2001) Multimerization of phosphorylated and non-phosphorylated ArcA is necessary for the response regulator function of the Arc two-component signal transduction system, J. Biol. Chem. 276, 40873-40879.
    • (2001) J. Biol. Chem , vol.276 , pp. 40873-40879
    • Jeon, Y.1    Lee, Y.S.2    Han, J.S.3    Kim, J.B.4    Hwang, D.S.5
  • 15
    • 0037215521 scopus 로고    scopus 로고
    • Residue R113 is essential for PhoP dimerization and function: A residue buried in the asymmetric PhoP dimer interface determined in the PhoPN three-dimensional crystal structure
    • Chen, Y., Birck, C., Samama, J. P., and Hulett, F. M. (2003) Residue R113 is essential for PhoP dimerization and function: a residue buried in the asymmetric PhoP dimer interface determined in the PhoPN three-dimensional crystal structure, J. Bacteriol. 185, 262-273.
    • (2003) J. Bacteriol , vol.185 , pp. 262-273
    • Chen, Y.1    Birck, C.2    Samama, J.P.3    Hulett, F.M.4
  • 16
    • 0038154011 scopus 로고    scopus 로고
    • Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily
    • Robinson, V. L., Wu, T., and Stock, A. M. (2003) Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily, J. Bacteriol. 185, 4186-4194.
    • (2003) J. Bacteriol , vol.185 , pp. 4186-4194
    • Robinson, V.L.1    Wu, T.2    Stock, A.M.3
  • 18
    • 0033599026 scopus 로고    scopus 로고
    • Structure of a transiently phosphorylated switch in bacterial signal transduction
    • Kern, D., Volkman, B. F., Luginbuhl, P., Nohaile, M. J., Kustu, S., and Wemmer, D. E. (1999) Structure of a transiently phosphorylated switch in bacterial signal transduction, Nature 40, 894-898.
    • (1999) Nature , vol.40 , pp. 894-898
    • Kern, D.1    Volkman, B.F.2    Luginbuhl, P.3    Nohaile, M.J.4    Kustu, S.5    Wemmer, D.E.6
  • 19
    • 0033584875 scopus 로고    scopus 로고
    • Phosphorylated aspartate in the structure of a response regulator protein
    • Lewis, R. J., Brannigan, J. A., Muchová, K., Barák, I., and Wilkinson, A. J. (1999) Phosphorylated aspartate in the structure of a response regulator protein, J. Mol. Biol. 294, 9-15.
    • (1999) J. Mol. Biol , vol.294 , pp. 9-15
    • Lewis, R.J.1    Brannigan, J.A.2    Muchová, K.3    Barák, I.4    Wilkinson, A.J.5
  • 20
    • 0034624879 scopus 로고    scopus 로고
    • The 1.9 Å resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY
    • Halkides, C. J., McEvoy, M. M., Casper, E., Matsumura, P., Volz, K., and Dahlquist, F. W. (2000) The 1.9 Å resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY, Biochemistry 39, 5280-5286.
    • (2000) Biochemistry , vol.39 , pp. 5280-5286
    • Halkides, C.J.1    McEvoy, M.M.2    Casper, E.3    Matsumura, P.4    Volz, K.5    Dahlquist, F.W.6
  • 21
    • 24344476732 scopus 로고    scopus 로고
    • Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states
    • Bachhawat, P., Swapna, G. V., Montelione, G. T., and Stock, A. M. (2005) Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states, Structure 13, 1353-1363.
    • (2005) Structure , vol.13 , pp. 1353-1363
    • Bachhawat, P.1    Swapna, G.V.2    Montelione, G.T.3    Stock, A.M.4
  • 22
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single domain signaling protein
    • Volkman, B. F., Lipson, D., Wemmer, D. E., and Kern, D. (2001) Two-state allosteric behavior in a single domain signaling protein, Science 291, 2429-2433.
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 23
    • 1942475365 scopus 로고    scopus 로고
    • Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states
    • Bent, C. J., Isaacs, N. W., Mitchell, T. J., and Riboldi-Tunnicliffe, A. (2004) Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states, J. Bacteriol. 186, 2872-2879.
    • (2004) J. Bacteriol , vol.186 , pp. 2872-2879
    • Bent, C.J.1    Isaacs, N.W.2    Mitchell, T.J.3    Riboldi-Tunnicliffe, A.4
  • 24
    • 18144411635 scopus 로고    scopus 로고
    • Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: A symmetric dimer mediated by the α4-β5-α5 face
    • Toro-Roman, A., Mack, T. R., and Stock, A. M. (2005) Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the α4-β5-α5 face, J. Mol. Biol. 349, 11-26.
    • (2005) J. Mol. Biol , vol.349 , pp. 11-26
    • Toro-Roman, A.1    Mack, T.R.2    Stock, A.M.3
  • 25
    • 28844432653 scopus 로고    scopus 로고
    • A common dimerization interface in bacterial response regulators KdpE and TorR
    • Toro-Roman, A., Wu, T., and Stock, A. M. (2005) A common dimerization interface in bacterial response regulators KdpE and TorR, Protein Sci. 14, 3077-3388.
    • (2005) Protein Sci , vol.14 , pp. 3077-3388
    • Toro-Roman, A.1    Wu, T.2    Stock, A.M.3
  • 26
    • 0022533109 scopus 로고
    • Nucleotide sequence of the phoB gene, the positive regulatory gene for the phosphate regulon of Escherichia coli K-12
    • Makino, K., Shinagawa, H., Amemura, M., and Nakata, A. (1986) Nucleotide sequence of the phoB gene, the positive regulatory gene for the phosphate regulon of Escherichia coli K-12, J. Mol. Biol. 190, 37-44.
    • (1986) J. Mol. Biol , vol.190 , pp. 37-44
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Nakata, A.4
  • 27
    • 0029157823 scopus 로고
    • Identification of base pairs important for OmpR-DNA interaction
    • Pratt, L. A., and Silhavy, T. J. (1995) Identification of base pairs important for OmpR-DNA interaction, Mol. Microbiol. 7, 565-573.
    • (1995) Mol. Microbiol , vol.7 , pp. 565-573
    • Pratt, L.A.1    Silhavy, T.J.2
  • 28
    • 0028862516 scopus 로고
    • Binding of the TorR regulator to cis-acting direct repeats activates tor operon expression
    • Simon, G., Jourlin, C., Ansaldi, M., Pascal, M. C., Chippaux, M., and Mejean, V. (1995) Binding of the TorR regulator to cis-acting direct repeats activates tor operon expression, Mol. Microbiol. 17, 971-980.
    • (1995) Mol. Microbiol , vol.17 , pp. 971-980
    • Simon, G.1    Jourlin, C.2    Ansaldi, M.3    Pascal, M.C.4    Chippaux, M.5    Mejean, V.6
  • 29
    • 0029858049 scopus 로고    scopus 로고
    • Transcriptional control mediated by the ArcA two-component response regultor protein of Escherichia coli: Characterization of DNA binding at target promoters
    • Lynch, A. S., and Lin, E. C. (1996) Transcriptional control mediated by the ArcA two-component response regultor protein of Escherichia coli: characterization of DNA binding at target promoters, J. Bacteriol. 178, 6238-6249.
    • (1996) J. Bacteriol , vol.178 , pp. 6238-6249
    • Lynch, A.S.1    Lin, E.C.2
  • 30
    • 0036583638 scopus 로고    scopus 로고
    • Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator
    • Blanco, A. G., Sola, M., Gomis-Ruth, F. X., and Coll, M. (2002) Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator, Structure 10, 701-713.
    • (2002) Structure , vol.10 , pp. 701-713
    • Blanco, A.G.1    Sola, M.2    Gomis-Ruth, F.X.3    Coll, M.4
  • 31
    • 0036174746 scopus 로고    scopus 로고
    • Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from
    • Buckler, D. R., Zhou, Y., and Stock, A. M. (2002) Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from, Thermotoga maritima, Structure 10, 153-164.
    • (2002) Thermotoga maritima, Structure , vol.10 , pp. 153-164
    • Buckler, D.R.1    Zhou, Y.2    Stock, A.M.3
  • 32
    • 33646898275 scopus 로고    scopus 로고
    • The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis
    • Nowak, E., Panjikar, S., Konarev, P., Svergun, D. I., and Tucker, P. A. (2006) The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis, J. Biol. Chem. 281, 9659-9666.
    • (2006) J. Biol. Chem , vol.281 , pp. 9659-9666
    • Nowak, E.1    Panjikar, S.2    Konarev, P.3    Svergun, D.I.4    Tucker, P.A.5
  • 33
    • 0344142378 scopus 로고    scopus 로고
    • Three-dimensional crystal structure of the transcription factor PhoB receiver domain
    • Solà, M., Gomis-Rüth, F. X., Serrano, L., González, A., and Coll, M. (1999) Three-dimensional crystal structure of the transcription factor PhoB receiver domain, J. Mol. Biol. 285, 675-687.
    • (1999) J. Mol. Biol , vol.285 , pp. 675-687
    • Solà, M.1    Gomis-Rüth, F.X.2    Serrano, L.3    González, A.4    Coll, M.5
  • 34
    • 0037215598 scopus 로고    scopus 로고
    • The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface
    • Birck, C., Chen, Y., Hulett, F. M., and Samama, J. P. (2003) The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface, J. Bacteriol. 185, 254-261.
    • (2003) J. Bacteriol , vol.185 , pp. 254-261
    • Birck, C.1    Chen, Y.2    Hulett, F.M.3    Samama, J.P.4
  • 35
    • 0030008674 scopus 로고    scopus 로고
    • Elements of signal transduction in Mycobacterium tuberculosis: In vitro phosphorylation and in vivo expression of the response regulator MtrA
    • Via, L. E., Curcic, R., Mudd, M. H., Dhandayuthapani, S., Ulmer, R. J., and Deretic, V. (1996) Elements of signal transduction in Mycobacterium tuberculosis: in vitro phosphorylation and in vivo expression of the response regulator MtrA, J. Bacteriol. 178, 3314-3321.
    • (1996) J. Bacteriol , vol.178 , pp. 3314-3321
    • Via, L.E.1    Curcic, R.2    Mudd, M.H.3    Dhandayuthapani, S.4    Ulmer, R.J.5    Deretic, V.6
  • 36
    • 0034130852 scopus 로고    scopus 로고
    • An essential two-component signal transduction system in Mycobacterium tuberculosis
    • Zahrt, T. C., and Deretic, V. (2000) An essential two-component signal transduction system in Mycobacterium tuberculosis, J. Bacteriol. 182, 3832-3838.
    • (2000) J. Bacteriol , vol.182 , pp. 3832-3838
    • Zahrt, T.C.1    Deretic, V.2
  • 38
    • 0034238106 scopus 로고    scopus 로고
    • 32P]-phosphoramidate for use as a low molecular weight phosphodonor reagent
    • 32P]-phosphoramidate for use as a low molecular weight phosphodonor reagent, Anal. Biochem. 283, 222-227.
    • (2000) Anal. Biochem , vol.283 , pp. 222-227
    • Buckler, D.R.1    Stock, A.M.2
  • 40
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 41
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0
    • Bricogne, G., Vonrhein, C., Flensburg, C., Schiltz, M., and Paciorek, W. (2003) Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0, Acta Crystallogr., Sect. D 59, 2023-2030.
    • (2003) Acta Crystallogr., Sect. D , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 42
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris, R. J., Perrakis, A., and Lamzin, V. S. (2003) ARP/wARP and automatic interpretation of protein electron density maps, Methods Enzymol. 374, 229-244.
    • (2003) Methods Enzymol , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 43
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics, Acta Crystallogr., Sect. D 60, 2126-2132.
    • (2004) Acta Crystallogr., Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 45
    • 33645885336 scopus 로고    scopus 로고
    • Modulation of Mycobacterium tuberculosis proliferation by MtrA, an essential two-component response regulator
    • Fol, M., Chauhan, A., Nair, N. K., Maloney, E., Moomey, M., Jagannath, C., Madiraju, M. V., and Rajagopalan, M. (2006) Modulation of Mycobacterium tuberculosis proliferation by MtrA, an essential two-component response regulator, Mol. Microbiol. 60, 643-657.
    • (2006) Mol. Microbiol , vol.60 , pp. 643-657
    • Fol, M.1    Chauhan, A.2    Nair, N.K.3    Maloney, E.4    Moomey, M.5    Jagannath, C.6    Madiraju, M.V.7    Rajagopalan, M.8
  • 46
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 47
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A., and Bacon, D. J. (1997) Raster3D: photorealistic molecular graphics, Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 49
    • 33744502092 scopus 로고    scopus 로고
    • Small revisions to predicted distances around metal sites in proteins
    • Harding, M. M. (2006) Small revisions to predicted distances around metal sites in proteins, Acta Crystallogr., Sect. D 62, 678-682.
    • (2006) Acta Crystallogr., Sect. D , vol.62 , pp. 678-682
    • Harding, M.M.1
  • 50
    • 0028131766 scopus 로고
    • OmpR mutants specifically defective for transcriptional activation
    • Pratt, L. A., and Silhavy, T. J. (1994) OmpR mutants specifically defective for transcriptional activation, J. Mol. Biol. 243, 579-594.
    • (1994) J. Mol. Biol , vol.243 , pp. 579-594
    • Pratt, L.A.1    Silhavy, T.J.2
  • 51
    • 0026512864 scopus 로고
    • Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors
    • Lukat, G. S., McCleary, W. R., Stock, A. M., and Stock, J. B. (1992) Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors, Proc. Natl. Acad. Sci. U.S.A. 89, 718-722.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 718-722
    • Lukat, G.S.1    McCleary, W.R.2    Stock, A.M.3    Stock, J.B.4
  • 54
    • 0032739281 scopus 로고    scopus 로고
    • C-terminal DN+A binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli
    • Ames, S. K., Frankema, N., and Kenney, L. J. (1999) C-terminal DN+A binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 96, 11792-11797.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 11792-11797
    • Ames, S.K.1    Frankema, N.2    Kenney, L.J.3
  • 55
    • 0035933040 scopus 로고    scopus 로고
    • Conformational coupling in the chemotaxis response regulator CheY
    • Schuster, M., Silversmith, R. E., and Bourret, R. B. (2001) Conformational coupling in the chemotaxis response regulator CheY, Proc. Natl. Acad. Sci. U.S.A. 98, 6003-6008.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 6003-6008
    • Schuster, M.1    Silversmith, R.E.2    Bourret, R.B.3
  • 56
    • 0037031925 scopus 로고    scopus 로고
    • The linker region plays an important role in the inter-domain communication of the response regulator OmpR
    • Mattison, K., Oropeza, R., and Kenney, L. J. (2002) The linker region plays an important role in the inter-domain communication of the response regulator OmpR, J. Biol. Chem. 277, 32714-32721.
    • (2002) J. Biol. Chem , vol.277 , pp. 32714-32721
    • Mattison, K.1    Oropeza, R.2    Kenney, L.J.3
  • 57
    • 0037216806 scopus 로고    scopus 로고
    • Interdomain linkers of homologous response regulators determine their mechanism of action
    • Walthers, D., Trail, V. K., and Kenney, L. J. (2003) Interdomain linkers of homologous response regulators determine their mechanism of action, J. Bacteriol. 185, 317-324.
    • (2003) J. Bacteriol , vol.185 , pp. 317-324
    • Walthers, D.1    Trail, V.K.2    Kenney, L.J.3
  • 58
    • 0032539671 scopus 로고    scopus 로고
    • Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain
    • Djordjevic, S., Goudreau, P. N., Xu, Q., Stock, A. M., and West, A. H. (1998) Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain, Proc. Natl. Acad. Sci. U.S.A. 95, 1381-1386.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 1381-1386
    • Djordjevic, S.1    Goudreau, P.N.2    Xu, Q.3    Stock, A.M.4    West, A.H.5
  • 59
    • 0034460872 scopus 로고    scopus 로고
    • The unphosphorylated receiver domain of PhoB silences the activity of its output domain
    • Ellison, D. W., and McCleary, W. R. (2000) The unphosphorylated receiver domain of PhoB silences the activity of its output domain, J. Bacteriol. 182, 6592-6597.
    • (2000) J. Bacteriol , vol.182 , pp. 6592-6597
    • Ellison, D.W.1    McCleary, W.R.2
  • 60
    • 0027962398 scopus 로고
    • Gene activation by the Escherichia coli positive regulator, OmpR: Phosphorylation-independent mechanism of activation by an OmpR mutant
    • Tsuzuki, M., Aiba, H., and Mizuno, T. (1994) Gene activation by the Escherichia coli positive regulator, OmpR: phosphorylation-independent mechanism of activation by an OmpR mutant, J. Mol. Biol. 242, 607-613.
    • (1994) J. Mol. Biol , vol.242 , pp. 607-613
    • Tsuzuki, M.1    Aiba, H.2    Mizuno, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.