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Volumn 44, Issue 6, 2005, Pages 1960-1970

Understanding GFP chromophore biosynthesis: Controlling backbone cyclization and modifying post-translational chemistry

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; CARBONYLATION; CHEMICAL BONDS; CRYSTALLOGRAPHY; HYDROGEN; NITROGEN; PROTEINS;

EID: 13544256284     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0479205     Document Type: Article
Times cited : (69)

References (42)
  • 1
    • 0033942582 scopus 로고    scopus 로고
    • Novel cofactors via post-translational modification of enzyme active sites
    • Okeley, N. M., and van der Donk, W. A. (2000) Novel cofactors via post-translational modification of enzyme active sites, Chem. Biol. 7, R159-R171.
    • (2000) Chem. Biol. , vol.7
    • Okeley, N.M.1    Van Der Donk, W.A.2
  • 2
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormö, M., Cubitt, A. B., Kallio, K., Gross, L. A., Tsien, R. Y., and Remington, S. J. (1996) Crystal structure of the Aequorea victoria green fluorescent protein, Science 273, 1392-1395.
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormö, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 3
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang, F., Moss, L. G., and Phillips, G. N., 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
  • 4
    • 0035478435 scopus 로고    scopus 로고
    • Methylidene-imidazolone: A novel electrophile for substrate activation
    • Poppe, L. (2001) Methylidene-imidazolone: A novel electrophile for substrate activation, Curr. Opin. Chem. Biol. 5, 512-524.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 512-524
    • Poppe, L.1
  • 5
    • 1242341209 scopus 로고    scopus 로고
    • Discovery and role of methylidene imidazolone, a highly electrophilic prosthetic group
    • Retey, J. (2003) Discovery and role of methylidene imidazolone, a highly electrophilic prosthetic group, Biochim. Biophys. Acta 1647, 179-184.
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 179-184
    • Retey, J.1
  • 6
    • 0034796862 scopus 로고    scopus 로고
    • Methylidene-imidazolone (MIO) from histidine and phenylalanine ammonia-lyase
    • Langer, B., Langer, M., and Retey, J. (2001) Methylidene-imidazolone (MIO) from histidine and phenylalanine ammonia-lyase, Adv. Protein Chem. 58, 175-214.
    • (2001) Adv. Protein Chem. , vol.58 , pp. 175-214
    • Langer, B.1    Langer, M.2    Retey, J.3
  • 7
    • 0041154057 scopus 로고    scopus 로고
    • Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile
    • Schwede, T. F., Retey, J., and Schulz, G. E. (1999) Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile, Biochemistry 38, 5355-5361.
    • (1999) Biochemistry , vol.38 , pp. 5355-5361
    • Schwede, T.F.1    Retey, J.2    Schulz, G.E.3
  • 8
    • 4444306767 scopus 로고    scopus 로고
    • Crystal structure of phenylalanine ammonia lyase: Multiple helix dipoles implicated in catalysis
    • Calabrese, J. C., Jordan, D. B., Boodhoo, A., Sariaslani, S., and Vannelli, T. (2004) Crystal structure of phenylalanine ammonia lyase: Multiple helix dipoles implicated in catalysis, Biochemistry 43, 11403-11416.
    • (2004) Biochemistry , vol.43 , pp. 11403-11416
    • Calabrese, J.C.1    Jordan, D.B.2    Boodhoo, A.3    Sariaslani, S.4    Vannelli, T.5
  • 9
    • 0038288848 scopus 로고    scopus 로고
    • A novel 4-methylideneimidazole-5-one-containing tyrosine amino-mutase in enediyne antitumor antibiotic C-1027 biosynthesis
    • Christenson, S. D., Liu, W., Toney, M. D., and Shen, B. (2003) A novel 4-methylideneimidazole-5-one-containing tyrosine amino-mutase in enediyne antitumor antibiotic C-1027 biosynthesis, J. Am. Chem. Soc. 125, 6062-6063.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6062-6063
    • Christenson, S.D.1    Liu, W.2    Toney, M.D.3    Shen, B.4
  • 10
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. (1998) The green fluorescent protein, Annu. Rev. Biochem. 67, 509-544.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 11
    • 0036489443 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP): Applications, structure, and related photophysical behavior
    • Zimmer, M. (2002) Green fluorescent protein (GFP): Applications, structure, and related photophysical behavior, Chem. Rev. 102, 759-782.
    • (2002) Chem. Rev. , vol.102 , pp. 759-782
    • Zimmer, M.1
  • 14
    • 0028580734 scopus 로고
    • Wavelength mutations and posttranslational autooxidation of the green fluorescent protein
    • Heim, R., Prasher, D. C., and Tsien, R. Y. (1994) Wavelength mutations and posttranslational autooxidation of the green fluorescent protein, Proc. Natl. Acad. Sci. U.S.A. 91, 12501-12504.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12501-12504
    • Heim, R.1    Prasher, D.C.2    Tsien, R.Y.3
  • 15
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths, and fluorescence resonance energy transfer
    • Heim, R., and Tsien, R. Y. (1996) Engineering green fluorescent protein for improved brightness, longer wavelengths, and fluorescence resonance energy transfer. Curr. Biol. 6, 178-182.
    • (1996) Curr. Biol. , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 16
    • 0025820866 scopus 로고
    • Histidase and histidinemia. Clinical and molecular considerations
    • Taylor, R. G., Levy, H. L., and McInnes, R. R. (1991) Histidase and histidinemia. Clinical and molecular considerations, Mol. Biol. Med. 8, 101-116.
    • (1991) Mol. Biol. Med. , vol.8 , pp. 101-116
    • Taylor, R.G.1    Levy, H.L.2    McInnes, R.R.3
  • 17
    • 0033514997 scopus 로고    scopus 로고
    • A different approach to treatment of phenylketonuria: Phenylalanine degradation with recombinant phenylalanine ammonia lyase
    • Sarkissian, C. N., Shao, Z., Blain, F., Peevers, R., Su, H., Heft, R., Chang, T. M., and Scriver, C. R. (1999) A different approach to treatment of phenylketonuria: Phenylalanine degradation with recombinant phenylalanine ammonia lyase, Proc. Natl. Acad. Sci. U.S.A. 96, 2339-2344.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 2339-2344
    • Sarkissian, C.N.1    Shao, Z.2    Blain, F.3    Peevers, R.4    Su, H.5    Heft, R.6    Chang, T.M.7    Scriver, C.R.8
  • 19
    • 0031006611 scopus 로고    scopus 로고
    • Chromophore formation in green fluorescent protein
    • Reid, B. G., and Flynn, G. C. (1997) Chromophore formation in green fluorescent protein, Biochemistry 36, 6786-6791.
    • (1997) Biochemistry , vol.36 , pp. 6786-6791
    • Reid, B.G.1    Flynn, G.C.2
  • 20
    • 0036154018 scopus 로고    scopus 로고
    • Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase
    • Baedeker, M., and Schulz, G. E. (2002) Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase, Structure 10, 61-67.
    • (2002) Structure , vol.10 , pp. 61-67
    • Baedeker, M.1    Schulz, G.E.2
  • 21
    • 11844250759 scopus 로고    scopus 로고
    • The crystal structure of the Y66L variant of green fluorescent protein supports a cyclization-oxidation-dehydration mechanism for chromophore maturation
    • Rosenow, M. A., Huffman, H. A., Phail, M. E., and Wachter, R. M. (2004) The crystal structure of the Y66L variant of green fluorescent protein supports a cyclization-oxidation-dehydration mechanism for chromophore maturation, Biochemistry 43, 4464-4472.
    • (2004) Biochemistry , vol.43 , pp. 4464-4472
    • Rosenow, M.A.1    Huffman, H.A.2    Phail, M.E.3    Wachter, R.M.4
  • 22
    • 0035152671 scopus 로고    scopus 로고
    • Theoretical study of the mechanism of peptide ring formation in green fluorescent protein
    • Siegbahn, P. E. M., Wirstam, M., and Zimmer, M. (2001) Theoretical study of the mechanism of peptide ring formation in green fluorescent protein, Int. J. Quantum Chem. 81, 169-186.
    • (2001) Int. J. Quantum Chem. , vol.81 , pp. 169-186
    • Siegbahn, P.E.M.1    Wirstam, M.2    Zimmer, M.3
  • 24
    • 0033674629 scopus 로고    scopus 로고
    • The structural basis for red fluorescence in the tetrameric GFP homolog DsRed
    • Wall, M. A., Socolich, M., and Ranganathan, R. (2000) The structural basis for red fluorescence in the tetrameric GFP homolog DsRed, Nature Struct. Biol. 7, 1133-1138.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 1133-1138
    • Wall, M.A.1    Socolich, M.2    Ranganathan, R.3
  • 25
    • 0035895225 scopus 로고    scopus 로고
    • Refined crystal structure of DsRed, a red fluorescent protein from coral, at 2.0 Å resolution
    • Yarbrough, D., Wachter, R. M., Kallio, K., Matz, M. V., and Remington, S. J. (2001) Refined crystal structure of DsRed, a red fluorescent protein from coral, at 2.0 Å resolution, Proc. Natl. Acad. Sci. U.S.A. 98, 462-467.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 462-467
    • Yarbrough, D.1    Wachter, R.M.2    Kallio, K.3    Matz, M.V.4    Remington, S.J.5
  • 26
    • 0032515404 scopus 로고    scopus 로고
    • A computational analysis of the unique protein-induced tight turn that results in posttranslational chromophore formation in green fluorescent protein
    • Branchini, B. R., Nemser, A. R., and Zimmer, M. (1998) A computational analysis of the unique protein-induced tight turn that results in posttranslational chromophore formation in green fluorescent protein, J. Am. Chem. Soc 120, 1-6.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 1-6
    • Branchini, B.R.1    Nemser, A.R.2    Zimmer, M.3
  • 27
    • 0034824716 scopus 로고    scopus 로고
    • Computational analysis of the autocatalytic posttranslational cyclization observed in histidine ammonia-lyase. A comparison with green fluorescent protein
    • Donnelly, M., Fedeles, F., Wirstam, M., Siegbahn, P. E., and Zimmer, M. (2001) Computational analysis of the autocatalytic posttranslational cyclization observed in histidine ammonia-lyase. A comparison with green fluorescent protein, J. Am. Chem. Soc. 123, 4679-4686.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 4679-4686
    • Donnelly, M.1    Fedeles, F.2    Wirstam, M.3    Siegbahn, P.E.4    Zimmer, M.5
  • 28
    • 0142027791 scopus 로고    scopus 로고
    • Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures
    • Barondeau, D. P., Putnam, C. D., Kassmann, C. J., Tainer, J. A., and Getzoff, E. D. (2003) Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures, Proc. Natl. Acad. Sci. U.S.A. 100, 12111-12116.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12111-12116
    • Barondeau, D.P.1    Putnam, C.D.2    Kassmann, C.J.3    Tainer, J.A.4    Getzoff, E.D.5
  • 29
    • 0028921834 scopus 로고
    • Improved green fluorescence
    • Heim, R., Cubitt, A. B., and Tsien, R. Y. (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
  • 30
    • 0036223618 scopus 로고    scopus 로고
    • Structures of two histidine ammonia-lyase modifications and implications for the catalytic mechanism
    • Baedeker, M., and Schulz, G. E. (2002) Structures of two histidine ammonia-lyase modifications and implications for the catalytic mechanism, Eur. J. Biochem. 269, 1790-1797.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1790-1797
    • Baedeker, M.1    Schulz, G.E.2
  • 32
    • 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, Macromol. Crystallogr., Part A 276, 307-326.
    • (1997) Macromol. Crystallogr., Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: An automated package for molecular replacement, Acta Crystallogr., Sect. A 50, 157-163.
    • (1994) Acta Crystallogr., Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 34
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. (1999) XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density, J. Struct. Biol. 125, 156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 36
    • 0010641246 scopus 로고    scopus 로고
    • High-resolution structure refinement
    • Oxford University Press, New York
    • Sheldrick, G. M. (1997) High-resolution structure refinement, in Crystallographic Computing, Oxford University Press, New York.
    • (1997) Crystallographic Computing
    • Sheldrick, G.M.1
  • 37
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger, A. T. (1992) The free R value: A novel statistical quantity for assessing the accuracy of crystal structures, Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brunger, A.T.1
  • 38
    • 0033531970 scopus 로고    scopus 로고
    • Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products
    • Bruns, C. M., Hubatsch, I., Ridderstrom, M., Mannervik, B., and Tainer, J. A. (1999) Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products, J. Mol. Biol. 288, 427-439.
    • (1999) J. Mol. Biol. , vol.288 , pp. 427-439
    • Bruns, C.M.1    Hubatsch, I.2    Ridderstrom, M.3    Mannervik, B.4    Tainer, J.A.5
  • 39
    • 0032532156 scopus 로고    scopus 로고
    • Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein
    • Wachter, R. M., Elsliger, M., Kallio, K., Hanson, G. T., and Remington, S. J. (1998) Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein, Structure 6, 1267-1277.
    • (1998) Structure , vol.6 , pp. 1267-1277
    • Wachter, R.M.1    Elsliger, M.2    Kallio, K.3    Hanson, G.T.4    Remington, S.J.5
  • 40
    • 0037432318 scopus 로고    scopus 로고
    • Backbone dynamics of green fluorescent protein and the effect of histidine 148 substitution
    • Seifert, M. H., Georgescu, J., Ksiazek, D., Smialowski, P., Rehm, T., Steipe, B., and Holak, T. A. (2003) Backbone dynamics of green fluorescent protein and the effect of histidine 148 substitution, Biochemistry 42, 2500-2512.
    • (2003) Biochemistry , vol.42 , pp. 2500-2512
    • Seifert, M.H.1    Georgescu, J.2    Ksiazek, D.3    Smialowski, P.4    Rehm, T.5    Steipe, B.6    Holak, T.A.7
  • 42
    • 0030886443 scopus 로고    scopus 로고
    • Rational protein design: Combining theory and experiment
    • Hellinga, H. W. (1997) Rational protein design: Combining theory and experiment, Proc. Natl. Acad. Sci. U.S.A. 94, 10015-10017.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10015-10017
    • Hellinga, H.W.1


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