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Volumn 7, Issue 10, 2012, Pages

Crystal Structure of Enhanced Green Fluorescent Protein to 1.35 Å Resolution Reveals Alternative Conformations for Glu222

Author keywords

[No Author keywords available]

Indexed keywords

ENHANCED GREEN FLUORESCENT PROTEIN; GLUTAMIC ACID;

EID: 84867619172     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047132     Document Type: Article
Times cited : (112)

References (26)
  • 1
    • 34548576414 scopus 로고
    • Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea
    • Shimomura O, Johnson FH, Saiga Y, (1962) Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J Cell Comp Phys 59: 223-239.
    • (1962) J Cell Comp Phys , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 2
  • 3
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien RY, (1998) The green fluorescent protein. Ann Rev Biochem 67: 509-544.
    • (1998) Ann Rev Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 5
    • 49449115068 scopus 로고    scopus 로고
    • GFP family: structural insights into spectral tuning
    • Pakhomov AA, Martynov VI, (2008) GFP family: structural insights into spectral tuning. Chem Biol 15: 755-764.
    • (2008) Chem Biol , vol.15 , pp. 755-764
    • Pakhomov, A.A.1    Martynov, V.I.2
  • 6
    • 33646026448 scopus 로고    scopus 로고
    • Reaction progress of chromophore biogenesis in green fluorescent protein
    • Zhang L, Patel HN, Lappe JW, Wachter RM, (2006) Reaction progress of chromophore biogenesis in green fluorescent protein. J Am Chem Soc 128: 4766-4772.
    • (2006) J Am Chem Soc , vol.128 , pp. 4766-4772
    • Zhang, L.1    Patel, H.N.2    Lappe, J.W.3    Wachter, R.M.4
  • 7
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang F, Moss LG, Phillips GN Jr, (1996) The molecular structure of green fluorescent protein. Nat Biotech 14: 1246-1251.
    • (1996) Nat Biotech , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr., G.N.3
  • 8
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, et al. (1996) Crystal structure of the Aequorea victoria green fluorescent protein. Science 273: 1392-1395.
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormo, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5
  • 9
    • 0028580734 scopus 로고
    • Wavelength mutations and posttranslational autoxidation of green fluorescent protein
    • Heim R, Prasher DC, Tsien RY, (1994) Wavelength mutations and posttranslational autoxidation of green fluorescent protein. Proc Natl Acad Sci USA 91: 12501-12504.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12501-12504
    • Heim, R.1    Prasher, D.C.2    Tsien, R.Y.3
  • 10
    • 0037418882 scopus 로고    scopus 로고
    • Development and use of fluorescent protein markers in living cells
    • Lippincott-Schwartz J, Patterson GH, (2003) Development and use of fluorescent protein markers in living cells. Science 300: 87-91.
    • (2003) Science , vol.300 , pp. 87-91
    • Lippincott-Schwartz, J.1    Patterson, G.H.2
  • 11
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack BP, Valdivia RH, Falkow S, (1996) FACS-optimized mutants of the green fluorescent protein (GFP). Gene 173: 33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 12
    • 0029909407 scopus 로고    scopus 로고
    • Optimized codon usage and chromophore mutations provide enhanced sensitivity with the green fluorescent protein
    • Yang TT, Cheng L, Kain SR, (1996) Optimized codon usage and chromophore mutations provide enhanced sensitivity with the green fluorescent protein. Nucleic Acids Res 24: 4592-4593.
    • (1996) Nucleic Acids Res , vol.24 , pp. 4592-4593
    • Yang, T.T.1    Cheng, L.2    Kain, S.R.3
  • 13
    • 79954425820 scopus 로고    scopus 로고
    • Stabilizing role of glutamic acid 222 in the structure of Enhanced Green Fluorescent Protein
    • Royant A, Noirclerc-Savoye M, (2011) Stabilizing role of glutamic acid 222 in the structure of Enhanced Green Fluorescent Protein. J Struc Biol 174: 385-390.
    • (2011) J Struc Biol , vol.174 , pp. 385-390
    • Royant, A.1    Noirclerc-Savoye, M.2
  • 14
    • 0030784698 scopus 로고    scopus 로고
    • Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy
    • Patterson GH, Knobel SM, Sharif WD, Kain SR, Piston DW, (1997) Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy. Biophys J 73: 2782-2790.
    • (1997) Biophys J , vol.73 , pp. 2782-2790
    • Patterson, G.H.1    Knobel, S.M.2    Sharif, W.D.3    Kain, S.R.4    Piston, D.W.5
  • 15
    • 1842787741 scopus 로고    scopus 로고
    • Probing the role of tryptophans in Aequorea victoria green fluorescent proteins with an expanded genetic code
    • Budisa N, Pal PP, Alefelder S, Birle P, Krywcun T, et al. (2004) Probing the role of tryptophans in Aequorea victoria green fluorescent proteins with an expanded genetic code. Biol Chem 385: 191-202.
    • (2004) Biol Chem , vol.385 , pp. 191-202
    • Budisa, N.1    Pal, P.P.2    Alefelder, S.3    Birle, P.4    Krywcun, T.5
  • 16
    • 45949083738 scopus 로고    scopus 로고
    • Synthetic biology of proteins: tuning GFPs folding and stability with fluoroproline
    • Steiner T, Hess P, Bae JH, Wiltschi B, Moroder L, et al. (2008) Synthetic biology of proteins: tuning GFPs folding and stability with fluoroproline. PloS One 3: e1680.
    • (2008) PloS One , vol.3
    • Steiner, T.1    Hess, P.2    Bae, J.H.3    Wiltschi, B.4    Moroder, L.5
  • 17
    • 0028921834 scopus 로고
    • Improved green fluorescence
    • Heim R, Cubitt AB, Tsien RY, (1995) Improved green fluorescence. Nature 373: 663-664.
    • (1995) Nature , vol.373 , pp. 663-664
    • Heim, R.1    Cubitt, A.B.2    Tsien, R.Y.3
  • 18
    • 0030953638 scopus 로고    scopus 로고
    • Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein
    • Brejc K, Sixma TK, Kitts PA, Kain SR, Tsien RY, et al. (1997) Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein. Proc Natl Acad Sci U S A 94: 2306-2311.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2306-2311
    • Brejc, K.1    Sixma, T.K.2    Kitts, P.A.3    Kain, S.R.4    Tsien, R.Y.5
  • 19
    • 35648978040 scopus 로고    scopus 로고
    • Ultrafast excited-state dynamics in the green fluorescent protein variant S65T/H148D. 1. Mutagenesis and structural studies
    • Shu X, Kallio K, Shi X, Abbyad P, Kanchanawong P, et al. (2007) Ultrafast excited-state dynamics in the green fluorescent protein variant S65T/H148D. 1. Mutagenesis and structural studies. Biochemistry 46: 12005-12013.
    • (2007) Biochemistry , vol.46 , pp. 12005-12013
    • Shu, X.1    Kallio, K.2    Shi, X.3    Abbyad, P.4    Kanchanawong, P.5
  • 20
    • 9744241605 scopus 로고    scopus 로고
    • Comparative studies on the structure and stability of fluorescent proteins EGFP, zFP506, mRFP1, "dimer2", and DsRed1
    • Stepanenko OV, Verkhusha VV, Kazakov VI, Shavlovsky MM, Kuznetsova IM, et al. (2004) Comparative studies on the structure and stability of fluorescent proteins EGFP, zFP506, mRFP1, "dimer2", and DsRed1. Biochemistry 43: 14913-14923.
    • (2004) Biochemistry , vol.43 , pp. 14913-14923
    • Stepanenko, O.V.1    Verkhusha, V.V.2    Kazakov, V.I.3    Shavlovsky, M.M.4    Kuznetsova, I.M.5
  • 21
    • 75649151032 scopus 로고    scopus 로고
    • xia2: an expert system for macromolecular crystallography data reduction
    • Winter G, (2010) xia2: an expert system for macromolecular crystallography data reduction. J App Crystallogr 43: 186-190.
    • (2010) J App Crystallogr , vol.43 , pp. 186-190
    • Winter, G.1
  • 22
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans PR, (2006) Scaling and assessment of data quality. Acta Cryst D62: 72-82.
    • (2006) Acta Cryst , vol.D62 , pp. 72-82
    • Evans, P.R.1
  • 23
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • CCP4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 25
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.