메뉴 건너뛰기




Volumn 349, Issue 1, 2005, Pages 223-237

The 2.1 Å crystal structure of the far-red fluorescent protein HcRed: Inherent conformational flexibility of the chromophore

Author keywords

Chromophore configuration; Fluorescent protein; HcRed; Structure

Indexed keywords

DIMER; FLUORESCENT PROTEIN; GLUTAMIC ACID; GLYCINE; GREEN FLUORESCENT PROTEIN; GREEN FLUORESCENT PROTEIN LIKE PROTEIN; MONOMER; TRIPEPTIDE; TYROSINE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; PHOTOPROTEIN; RED FLUORESCENT PROTEIN;

EID: 20444453728     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.03.020     Document Type: Article
Times cited : (74)

References (47)
  • 1
    • 0036793311 scopus 로고    scopus 로고
    • Family of the green fluorescent protein: Journey to the end of the rainbow
    • M.V. Matz, K.A. Lukyanov, and S.A. Lukyanov Family of the green fluorescent protein: journey to the end of the rainbow BioEssays 24 2002 953 959
    • (2002) BioEssays , vol.24 , pp. 953-959
    • Matz, M.V.1    Lukyanov, K.A.2    Lukyanov, S.A.3
  • 2
    • 11144357587 scopus 로고    scopus 로고
    • GFP-like proteins as ubiquitous metazoan superfamily: Evolution of functional features and structural complexity
    • D.A. Shagin, E.V. Barsova, Y.G. Yanushevich, A.F. Fradkov, K.A. Lukyanov, and Y.A. Labas GFP-like proteins as ubiquitous metazoan superfamily: evolution of functional features and structural complexity Mol. Biol. Evol. 21 2004 841 850
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 841-850
    • Shagin, D.A.1    Barsova, E.V.2    Yanushevich, Y.G.3    Fradkov, A.F.4    Lukyanov, K.A.5    Labas, Y.A.6
  • 3
    • 1542336956 scopus 로고    scopus 로고
    • The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins
    • V.V. Verkhusha, and K.A. Lukyanov The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins Nature Biotechnol. 22 2004 289 296
    • (2004) Nature Biotechnol. , vol.22 , pp. 289-296
    • Verkhusha, V.V.1    Lukyanov, K.A.2
  • 4
    • 0036823335 scopus 로고    scopus 로고
    • Green fluorescent protein-like proteins in reef Anthozoa animals
    • A. Miyawaki Green fluorescent protein-like proteins in reef Anthozoa animals Cell. Struct. Funct. 27 2002 343 347
    • (2002) Cell. Struct. Funct. , vol.27 , pp. 343-347
    • Miyawaki, A.1
  • 5
    • 0028580734 scopus 로고
    • Wavelength mutations and posttranslational autoxidation of green fluorescent protein
    • R. Heim, D.C. Prasher, and R.Y. Tsien Wavelength mutations and posttranslational autoxidation of green fluorescent protein Proc. Natl Acad. Sci. USA 91 1994 12501 12504
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12501-12504
    • Heim, R.1    Prasher, D.C.2    Tsien, R.Y.3
  • 6
    • 0036140797 scopus 로고    scopus 로고
    • Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222
    • J.J. van Thor, T. Gensch, K.J. Hellingwerf, and L.N. Johnson Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222 Nature Struct. Biol. 9 2002 37 41
    • (2002) Nature Struct. Biol. , vol.9 , pp. 37-41
    • Van Thor, J.J.1    Gensch, T.2    Hellingwerf, K.J.3    Johnson, L.N.4
  • 7
    • 0242361312 scopus 로고    scopus 로고
    • Photo-induced peptide cleavage in the green-to-red conversion of a fluorescent protein
    • H. Mizuno, T.K. Mal, K.I. Tong, R. Ando, T. Furuta, M. Ikura, and A. Miyawaki Photo-induced peptide cleavage in the green-to-red conversion of a fluorescent protein Mol. Cell. 12 2003 1051 1058
    • (2003) Mol. Cell. , vol.12 , pp. 1051-1058
    • Mizuno, H.1    Mal, T.K.2    Tong, K.I.3    Ando, R.4    Furuta, T.5    Ikura, M.6    Miyawaki, A.7
  • 9
    • 0242666241 scopus 로고    scopus 로고
    • The 2.0-Å crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor
    • J. Petersen, P.G. Wilmann, T. Beddoe, A.J. Oakley, R.J. Devenish, M. Prescott, and J. Rossjohn The 2.0-Å crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor J. Biol. Chem. 278 2003 44626 44631
    • (2003) J. Biol. Chem. , vol.278 , pp. 44626-44631
    • Petersen, J.1    Wilmann, P.G.2    Beddoe, T.3    Oakley, A.J.4    Devenish, R.J.5    Prescott, M.6    Rossjohn, J.7
  • 10
    • 0141749127 scopus 로고    scopus 로고
    • The 2.2 Å crystal structure of a pocilloporin pigment reveals a non-planar chromophore conformation
    • M. Prescott, M. Ling, T. Beddoe, A.J. Oakley, S. Dove, and O. Hoegh-Guldberg The 2.2 Å crystal structure of a pocilloporin pigment reveals a non-planar chromophore conformation Structure (Camb.) 11 2003 275 284
    • (2003) Structure (Camb.) , vol.11 , pp. 275-284
    • Prescott, M.1    Ling, M.2    Beddoe, T.3    Oakley, A.J.4    Dove, S.5    Hoegh-Guldberg, O.6
  • 11
    • 0033674629 scopus 로고    scopus 로고
    • The structural basis for red fluorescence in the tetrameric GFP homolog DsRed
    • M.A. Wall, M. Socolich, and R. Ranganathan The structural basis for red fluorescence in the tetrameric GFP homolog DsRed Nature Struct. Biol. 7 2000 1133 1138
    • (2000) Nature Struct. Biol. , vol.7 , pp. 1133-1138
    • Wall, M.A.1    Socolich, M.2    Ranganathan, R.3
  • 12
    • 13244299330 scopus 로고    scopus 로고
    • Variations on the GFP chromophore: A polypeptide fragmentation within the chromophore revealed in the 2.1 Å crystal structure of a non-fluorescent chromoprotein from Anemonia sulcata
    • P.G. Wilmann, J. Petersen, R.J. Devenish, M. Prescott, and J. Rossjohn Variations on the GFP chromophore: a polypeptide fragmentation within the chromophore revealed in the 2.1 Å crystal structure of a non-fluorescent chromoprotein from Anemonia sulcata J. Biol. Chem. 280 2004 2401 2404
    • (2004) J. Biol. Chem. , vol.280 , pp. 2401-2404
    • Wilmann, P.G.1    Petersen, J.2    Devenish, R.J.3    Prescott, M.4    Rossjohn, J.5
  • 15
    • 34248363186 scopus 로고    scopus 로고
    • Interconversion of Anthozoa GFP-like fluorescent and nonfluorescent proteins by mutagenesis
    • M.E. Bulina, D.M. Chudakov, N.N. Mudrik, and K.A. Lukyanov Interconversion of Anthozoa GFP-like fluorescent and nonfluorescent proteins by mutagenesis BMC Biochem. 3 2002 7
    • (2002) BMC Biochem. , vol.3 , pp. 7
    • Bulina, M.E.1    Chudakov, D.M.2    Mudrik, N.N.3    Lukyanov, K.A.4
  • 16
    • 3042691006 scopus 로고    scopus 로고
    • Common pathway for the red chromophore formation in fluorescent proteins and chromoproteins
    • V.V. Verkhusha, D.M. Chudakov, N.G. Gurskaya, S. Lukyanov, and K.A. Lukyanov Common pathway for the red chromophore formation in fluorescent proteins and chromoproteins Chem. Biol. 11 2004 845 854
    • (2004) Chem. Biol. , vol.11 , pp. 845-854
    • Verkhusha, V.V.1    Chudakov, D.M.2    Gurskaya, N.G.3    Lukyanov, S.4    Lukyanov, K.A.5
  • 18
    • 0031050445 scopus 로고    scopus 로고
    • Yeast-enhanced green fluorescent protein (yEGFP) a reporter of gene expression in Candida albicans
    • B.P. Cormack, G. Bertram, M. Egerton, N.A. Gow, S. Falkow, and A.J. Brown Yeast-enhanced green fluorescent protein (yEGFP) a reporter of gene expression in Candida albicans Microbiology 143 1997 303 311
    • (1997) Microbiology , vol.143 , pp. 303-311
    • Cormack, B.P.1    Bertram, G.2    Egerton, M.3    Gow, N.A.4    Falkow, S.5    Brown, A.J.6
  • 20
    • 0036897848 scopus 로고    scopus 로고
    • Aromatic interactions in model systems
    • M.L. Waters Aromatic interactions in model systems Curr. Opin. Chem. Biol. 6 2002 736 741
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 736-741
    • Waters, M.L.1
  • 22
    • 0037707298 scopus 로고    scopus 로고
    • A TDDFT study of the lowest excitation energies of polycyclic aromatic hydrocarbons
    • M. Parac, and S. Grimme A TDDFT study of the lowest excitation energies of polycyclic aromatic hydrocarbons Chem. Phys. 292 2003 11 21
    • (2003) Chem. Phys. , vol.292 , pp. 11-21
    • Parac, M.1    Grimme, S.2
  • 23
    • 4143087479 scopus 로고    scopus 로고
    • Theoretical analysis of the excited state properties of wybutine: A natural probe for transfer RNA dynamics
    • A. Lahiri, J. Uli_ny, and A. Laaksonen Theoretical analysis of the excited state properties of wybutine: a natural probe for transfer RNA dynamics Int. J. Mol. Sci. 5 2004 75 83
    • (2004) Int. J. Mol. Sci. , vol.5 , pp. 75-83
    • Lahiri, A.1    Uli-ny, J.2    Laaksonen, A.3
  • 25
    • 2342638866 scopus 로고    scopus 로고
    • Origin, nature and fate of the fluorescent state of green fluorescent protein chromophore at the CASPT2/CASSCF resolution
    • M.E. Martin, F. Negri, and M. Olivucci Origin, nature and fate of the fluorescent state of green fluorescent protein chromophore at the CASPT2/CASSCF resolution J. Am. Chem. Soc. 126 2004 5452 5464
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5452-5464
    • Martin, M.E.1    Negri, F.2    Olivucci, M.3
  • 27
    • 0037434722 scopus 로고    scopus 로고
    • Ab initio study of cis-trans photoisomerization in stilbene and ethylene
    • J. Quenneville, and T.J. Martínez Ab initio study of cis-trans photoisomerization in stilbene and ethylene J. Phys. Chem. 107A 2003 829 837
    • (2003) J. Phys. Chem. , vol.107 , pp. 829-837
    • Quenneville, J.1    Martínez, T.J.2
  • 28
    • 36549090986 scopus 로고
    • The torsional dynamics of cis-stillbene from resonance Raman intensities
    • A.B. Myers, and R.A. Mathies The torsional dynamics of cis-stillbene from resonance Raman intensities JCP 81 1984 1552 1558
    • (1984) JCP , vol.81 , pp. 1552-1558
    • Myers, A.B.1    Mathies, R.A.2
  • 29
    • 0000466256 scopus 로고
    • The spectroscopy and single vibronic level fluorescence quantum yields of jet cooled trans-stilbene and its van der Waals complexes
    • T.S. Zwier, M.E. Carasquillo, and D.H. Levy The spectroscopy and single vibronic level fluorescence quantum yields of jet cooled trans-stilbene and its van der Waals complexes J. Chem. Phys. 78 1983 5493 5505
    • (1983) J. Chem. Phys. , vol.78 , pp. 5493-5505
    • Zwier, T.S.1    Carasquillo, M.E.2    Levy, D.H.3
  • 30
    • 0001123199 scopus 로고
    • The viscosity dependence and reaction coordinate for isomerization of cis-stilbene
    • S. Abrash, S. Repinec, and R.M. Hochstrasser The viscosity dependence and reaction coordinate for isomerization of cis-stilbene J. Chem. Phys. 93 1990 1041 1053
    • (1990) J. Chem. Phys. , vol.93 , pp. 1041-1053
    • Abrash, S.1    Repinec, S.2    Hochstrasser, R.M.3
  • 31
    • 0032532156 scopus 로고    scopus 로고
    • Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein
    • R.M. Wachter, M.A. Elsliger, K. Kallio, G.T. Hanson, and S.J. Remington Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein Structure 6 1998 1267 1277
    • (1998) Structure , vol.6 , pp. 1267-1277
    • Wachter, R.M.1    Elsliger, M.A.2    Kallio, K.3    Hanson, G.T.4    Remington, S.J.5
  • 32
    • 0036434301 scopus 로고    scopus 로고
    • An approach for reducing unwanted oligomerisation of DsRed fusion proteins
    • P. Gavin, R.J. Devenish, and M. Prescott An approach for reducing unwanted oligomerisation of DsRed fusion proteins Biochem. Biophys. Res. Commun. 298 2002 707 713
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 707-713
    • Gavin, P.1    Devenish, R.J.2    Prescott, M.3
  • 35
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling Biophys. J. 78 2000 1606 1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 36
    • 1442274756 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition
    • J. Vistica, J. Dam, A. Balbo, E. Yikilmaz, R.A. Mariuzza, T.A. Rouault, and P. Schuck Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition Anal. Biochem. 326 2004 234 256
    • (2004) Anal. Biochem. , vol.326 , pp. 234-256
    • Vistica, J.1    Dam, J.2    Balbo, A.3    Yikilmaz, E.4    Mariuzza, R.A.5    Rouault, T.A.6    Schuck, P.7
  • 39
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 40
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 41
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. the role of exact exchange
    • A.D. Becke Density-functional thermochemistry. III. The role of exact exchange J. Chem. Phys. 98 1993 5648 5652
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 42
    • 36549091139 scopus 로고
    • Self-consistent molecular orbital methods 25. Supplementary functions for Gaussian basis sets
    • M.J. Frisch, J.A. Pople, and J.S. Binkley Self-consistent molecular orbital methods 25. Supplementary functions for Gaussian basis sets J. Chem. Phys. 80 1984 3265 3269
    • (1984) J. Chem. Phys. , vol.80 , pp. 3265-3269
    • Frisch, M.J.1    Pople, J.A.2    Binkley, J.S.3
  • 43
    • 0347170005 scopus 로고
    • Self-consistent molecular orbital methods. XII. Further extensions of gaussian-type basis sets for use in molecular orbital studies of organic molecules
    • W.J. Hehre, R. Ditchfield, and J.A. Pople Self-consistent molecular orbital methods. XII. Further extensions of gaussian-type basis sets for use in molecular orbital studies of organic molecules J. Chem. Phys. 56 1972 2257 2261
    • (1972) J. Chem. Phys. , vol.56 , pp. 2257-2261
    • Hehre, W.J.1    Ditchfield, R.2    Pople, J.A.3
  • 44
    • 26844534384 scopus 로고
    • Self-consistent molecular orbital methods. XX. a basis set for correlated wave functions
    • R. Krishnan, J.S. Binkley, and J.A. Pople Self-consistent molecular orbital methods. XX. A basis set for correlated wave functions J. Chem. Phys. 72 1980 650 654
    • (1980) J. Chem. Phys. , vol.72 , pp. 650-654
    • Krishnan, R.1    Binkley, J.S.2    Pople, J.A.3
  • 45
    • 3342998833 scopus 로고    scopus 로고
    • Excitations in time-dependent density-functional theory
    • H. Appel, E.K.U. Gross, and K. Burke Excitations in time-dependent density-functional theory Phys. Rev. Letters 90 2003 043005 [Epub]
    • (2003) Phys. Rev. Letters , vol.90
    • Appel, H.1    Gross, E.K.U.2    Burke, K.3
  • 46
    • 0035838240 scopus 로고    scopus 로고
    • Key concepts in time-dependent density functional theory
    • R. van Leeuwen Key concepts in time-dependent density functional theory Int. J. Modern Phys. B. 15 2001 1969 2023
    • (2001) Int. J. Modern Phys. B. , vol.15 , pp. 1969-2023
    • Van Leeuwen, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.