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Volumn 7, Issue 9, 2012, Pages

Trp RNA-Binding Attenuation Protein: Modifying Symmetry and Stability of a Circular Oligomer

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR PROTEIN OLIGOMER; MUTANT PROTEIN; PROTEIN; TRYPTOPHAN; TRYPTOPHAN RNA BINDING ATTENUATION PROTEIN; UNCLASSIFIED DRUG;

EID: 84866070607     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0044309     Document Type: Article
Times cited : (6)

References (30)
  • 1
    • 79958063382 scopus 로고    scopus 로고
    • Structural Insight into the Rotational Switching Mechanism of the Bacterial Flagellar Motor
    • Minamino T, Imada K, Kinoshita M, Nakamura S, Morimoto YV, et al. (2011) Structural Insight into the Rotational Switching Mechanism of the Bacterial Flagellar Motor. PLoS Biology 9(5): e1000616.
    • (2011) PLoS Biology , vol.9 , Issue.5
    • Minamino, T.1    Imada, K.2    Kinoshita, M.3    Nakamura, S.4    Morimoto, Y.V.5
  • 2
    • 0038053885 scopus 로고    scopus 로고
    • ATP synthesis driven by proton transport in F1F0-ATP synthase
    • Weber J, Senior AE, (2003) ATP synthesis driven by proton transport in F1F0-ATP synthase. Febs Letters 545(1): 61-70.
    • (2003) Febs Letters , vol.545 , Issue.1 , pp. 61-70
    • Weber, J.1    Senior, A.E.2
  • 3
    • 57649226492 scopus 로고    scopus 로고
    • The Bacteriophage DNA Packaging Motor
    • Rao VB, Feiss M, (2008) The Bacteriophage DNA Packaging Motor. Annual Review of Genetics 42: 647-81.
    • (2008) Annual Review of Genetics , vol.42 , pp. 647-681
    • Rao, V.B.1    Feiss, M.2
  • 4
    • 80051707836 scopus 로고    scopus 로고
    • The DNA-packaging nanomotor of tailed bacteriophages
    • Casjens SR, (2011) The DNA-packaging nanomotor of tailed bacteriophages. Nature Reviews Microbiology 9(9): 647-57.
    • (2011) Nature Reviews Microbiology , vol.9 , Issue.9 , pp. 647-657
    • Casjens, S.R.1
  • 5
    • 34247268349 scopus 로고    scopus 로고
    • Structural framework for DNA translocation via the viral portal protein
    • Lebedev AA, Krause MH, Isidro AL, Vagin AA, Orlova EV, et al. (2007) Structural framework for DNA translocation via the viral portal protein. Embo Journal 26(7): 1984-94.
    • (2007) Embo Journal , vol.26 , Issue.7 , pp. 1984-1994
    • Lebedev, A.A.1    Krause, M.H.2    Isidro, A.L.3    Vagin, A.A.4    Orlova, E.V.5
  • 6
    • 33749608423 scopus 로고    scopus 로고
    • The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar typhimurium
    • Thomas DR, Francis NR, Xu C, DeRosier DJ, (2006) The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar typhimurium. Journal of Bacteriology 188(20): 7039-48.
    • (2006) Journal of Bacteriology , vol.188 , Issue.20 , pp. 7039-7048
    • Thomas, D.R.1    Francis, N.R.2    Xu, C.3    DeRosier, D.J.4
  • 7
    • 70449556810 scopus 로고    scopus 로고
    • Translocation of double-stranded DNA through membrane-adapted phi29 motor protein nanopores
    • Wendell D, Jing P, Geng J, Subramaniam V, Lee TJ, et al. (2009) Translocation of double-stranded DNA through membrane-adapted phi29 motor protein nanopores. Nature Nanotechnology 4(11): 765-72.
    • (2009) Nature Nanotechnology , vol.4 , Issue.11 , pp. 765-772
    • Wendell, D.1    Jing, P.2    Geng, J.3    Subramaniam, V.4    Lee, T.J.5
  • 8
    • 0033575897 scopus 로고    scopus 로고
    • Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA
    • Antson AA, Dodson EJ, Dodson G, Greaves RB, Chen XP, et al. (1999) Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA. Nature 401(6750): 235-42.
    • (1999) Nature , vol.401 , Issue.6750 , pp. 235-242
    • Antson, A.A.1    Dodson, E.J.2    Dodson, G.3    Greaves, R.B.4    Chen, X.P.5
  • 9
    • 80053449593 scopus 로고    scopus 로고
    • How to Change the Oligomeric State of a Circular Protein Assembly: Switch from 11-Subunit to 12-Subunit TRAP Suggests a General Mechanism
    • Chen C-S, Smits C, Dodson GG, Shevtsov MB, Merlino N, et al. (2011) How to Change the Oligomeric State of a Circular Protein Assembly: Switch from 11-Subunit to 12-Subunit TRAP Suggests a General Mechanism. PLoS ONE 6(10): e25296.
    • (2011) PLoS ONE , vol.6 , Issue.10
    • Chen, C.-S.1    Smits, C.2    Dodson, G.G.3    Shevtsov, M.B.4    Merlino, N.5
  • 11
    • 36049023540 scopus 로고    scopus 로고
    • Using the ring-shaped protein TRAP to capture and confine gold nanodots on a surface
    • Heddle JG, Fujiwara I, Yamadaki H, Yoshii S, Nishio K, et al. (2007) Using the ring-shaped protein TRAP to capture and confine gold nanodots on a surface. Small 3(11): 1950-6.
    • (2007) Small , vol.3 , Issue.11 , pp. 1950-1956
    • Heddle, J.G.1    Fujiwara, I.2    Yamadaki, H.3    Yoshii, S.4    Nishio, K.5
  • 12
    • 70349442592 scopus 로고    scopus 로고
    • A Self-Assembled Protein Nanotube with High Aspect Ratio
    • Miranda FF, Iwasaki K, Akashi S, Sumitomo K, Kobayashi M, et al. (2009) A Self-Assembled Protein Nanotube with High Aspect Ratio. Small 5(18): 2077-84.
    • (2009) Small , vol.5 , Issue.18 , pp. 2077-2084
    • Miranda, F.F.1    Iwasaki, K.2    Akashi, S.3    Sumitomo, K.4    Kobayashi, M.5
  • 13
    • 33746906309 scopus 로고    scopus 로고
    • Thermodynamics of tryptophan-mediated activation of the trp RNA-binding attenuation protein
    • McElroy CA, Manfredo A, Gollnick P, Foster MP, (2006) Thermodynamics of tryptophan-mediated activation of the trp RNA-binding attenuation protein. Biochemistry 45(25): 7844-53.
    • (2006) Biochemistry , vol.45 , Issue.25 , pp. 7844-7853
    • McElroy, C.A.1    Manfredo, A.2    Gollnick, P.3    Foster, M.P.4
  • 14
    • 0036416144 scopus 로고    scopus 로고
    • TROSY-NMR studies of the 91 kDa TRAP protein reveal allosteric control of a gene regulatory protein by ligand-altered flexibility
    • McElroy C, Manfredo A, Wendt A, Gollnick P, Foster M, (2002) TROSY-NMR studies of the 91 kDa TRAP protein reveal allosteric control of a gene regulatory protein by ligand-altered flexibility. Journal of Molecular Biology 323(3): 463-73.
    • (2002) Journal of Molecular Biology , vol.323 , Issue.3 , pp. 463-473
    • McElroy, C.1    Manfredo, A.2    Wendt, A.3    Gollnick, P.4    Foster, M.5
  • 15
    • 79952168694 scopus 로고    scopus 로고
    • Crystal structure of unliganded TRAP: implications for dynamic allostery
    • Malay AD, Watanabe M, Heddle JG, Tame JRH, (2011) Crystal structure of unliganded TRAP: implications for dynamic allostery. Biochemical Journal 434: 427-34.
    • (2011) Biochemical Journal , vol.434 , pp. 427-434
    • Malay, A.D.1    Watanabe, M.2    Heddle, J.G.3    Tame, J.R.H.4
  • 16
    • 28844474910 scopus 로고    scopus 로고
    • Evidence for macromolecular protein rings in the absence of bulk water
    • Ruotolo BT, Giles K, Campuzano I, Sandercock AM, Bateman RH, et al. (2005) Evidence for macromolecular protein rings in the absence of bulk water. Science 310(5754): 1658-61.
    • (2005) Science , vol.310 , Issue.5754 , pp. 1658-1661
    • Ruotolo, B.T.1    Giles, K.2    Campuzano, I.3    Sandercock, A.M.4    Bateman, R.H.5
  • 17
    • 0033022150 scopus 로고    scopus 로고
    • Regulatory features of the trp operon and the crystal structure of the trp RNA-binding attenuation protein from Bacillus stearothermophilus
    • Chen XP, Antson AA, Yang M, Li P, Baumann C, et al. (1999) Regulatory features of the trp operon and the crystal structure of the trp RNA-binding attenuation protein from Bacillus stearothermophilus. Journal of Molecular Biology 289(4): 1003-16.
    • (1999) Journal of Molecular Biology , vol.289 , Issue.4 , pp. 1003-1016
    • Chen, X.P.1    Antson, A.A.2    Yang, M.3    Li, P.4    Baumann, C.5
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography, Pt A 276: 307-26.
    • (1997) Macromolecular Crystallography , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 20
    • 0028103275 scopus 로고
    • The CCP4 Suite - programs for protein crystallography. Acta Crystallographica Section D-Biological Crystallography
    • Bailey S, (1994) The CCP4 Suite- programs for protein crystallography. Acta Crystallographica Section D-Biological Crystallography. 50: 760-3.
    • (1994) , vol.50 , pp. 760-763
    • Bailey, S.1
  • 25
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf RM, (1997) An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. Journal of Molecular Graphics & Modelling 15(2): 132-134.
    • (1997) Journal of Molecular Graphics & Modelling , vol.15 , Issue.2 , pp. 132-134
    • Esnouf, R.M.1
  • 28
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen FH, Berglund H, Vedadi M, (2007) The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nature Protocols 2(9): 2212-21.
    • (2007) Nature Protocols , vol.2 , Issue.9 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 29
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson UB, Hallberg BM, DeTitta GT, Dekker N, Nordlund P, (2006) Thermofluor-based high-throughput stability optimization of proteins for structural studies. Analytical Biochemistry 357(2): 289-98.
    • (2006) Analytical Biochemistry , vol.357 , Issue.2 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    DeTitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 30
    • 1542705098 scopus 로고    scopus 로고
    • Characterization of a trp RNA-binding attenuation protein (TRAP) mutant with tryptophan independent RNA binding activity
    • Li PTX, Gollnick P, (2004) Characterization of a trp RNA-binding attenuation protein (TRAP) mutant with tryptophan independent RNA binding activity. Journal of Molecular Biology 335(3): 707-22.
    • (2004) Journal of Molecular Biology , vol.335 , Issue.3 , pp. 707-722
    • Li, P.T.X.1    Gollnick, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.