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Volumn 434, Issue 7033, 2005, Pages 612-618

Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; FREE ENERGY; MOLECULAR STRUCTURE; MUTAGENESIS; OXIDATION; X RAY ANALYSIS;

EID: 15844379169     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03458     Document Type: Article
Times cited : (296)

References (31)
  • 1
    • 0026701365 scopus 로고
    • The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)
    • Michaels, M. L. & Miller, J. H. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 174, 6321-6325 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 6321-6325
    • Michaels, M.L.1    Miller, J.H.2
  • 2
    • 0027324378 scopus 로고
    • Mutagenesis by 8-oxoguanine: An enemy within
    • Grollman, A. P. & Moriya, M. Mutagenesis by 8-oxoguanine: an enemy within. Trends Genet. 9, 246-249 (1993).
    • (1993) Trends Genet. , vol.9 , pp. 246-249
    • Grollman, A.P.1    Moriya, M.2
  • 3
    • 0035098395 scopus 로고    scopus 로고
    • Rates of base excision repair are not solely dependent on levels of initiating enzymes
    • Cappelli, E. et al. Rates of base excision repair are not solely dependent on levels of initiating enzymes. Carcinogenesis 22, 387-393 (2001).
    • (2001) Carcinogenesis , vol.22 , pp. 387-393
    • Cappelli, E.1
  • 4
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • Bruner, S. D., Norman, D. P. & Verdine, G. L. Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature 403, 859-866 (2000).
    • (2000) Nature , vol.403 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.2    Verdine, G.L.3
  • 6
    • 0037452513 scopus 로고    scopus 로고
    • Structural and biochemical exploration of a critical amino acid in human 8-oxoguanine glycosylase
    • Norman, D. P., Chung, S. J. & Verdine, G. L. Structural and biochemical exploration of a critical amino acid in human 8-oxoguanine glycosylase. Biochemistry 42, 1564-1572 (2003).
    • (2003) Biochemistry , vol.42 , pp. 1564-1572
    • Norman, D.P.1    Chung, S.J.2    Verdine, G.L.3
  • 7
    • 0035900960 scopus 로고    scopus 로고
    • Coupling of substrate recognition and catalysis by a human base-excision DNA repair protein
    • Norman, D. P. G., Bruner, S. D. & Verdine, G. L. Coupling of substrate recognition and catalysis by a human base-excision DNA repair protein. J. Am. Chem. Soc. 123, 359-360 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 359-360
    • Norman, D.P.G.1    Bruner, S.D.2    Verdine, G.L.3
  • 8
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F. & Richmond, T. J. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389, 251-260 (1997).
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 9
    • 0033634983 scopus 로고    scopus 로고
    • Structure of BamHI bound to nonspecific DNA: A model for DNA sliding
    • Viadiu, H. & Aggarwal, A. K. Structure of BamHI bound to nonspecific DNA: a model for DNA sliding. Mol. Cell 5, 889-895 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 889-895
    • Viadiu, H.1    Aggarwal, A.K.2
  • 10
    • 0032510217 scopus 로고    scopus 로고
    • The hyperthermophile chromosomal protein Sac7d sharply kinks DNA
    • Robinson, H. et al. The hyperthermophile chromosomal protein Sac7d sharply kinks DNA. Nature 392, 202-205 (1998).
    • (1998) Nature , vol.392 , pp. 202-205
    • Robinson, H.1
  • 11
    • 0031718377 scopus 로고    scopus 로고
    • The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA
    • Gao, Y. G. et al. The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA. Nature Struct. Biol. 5, 782-786 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 782-786
    • Gao, Y.G.1
  • 12
    • 0034111063 scopus 로고    scopus 로고
    • Trapping of a catalytic HIV reverse transcriptase•template:primer complex through a disulfide bond
    • Huang, H., Harrison, S. C, & Verdine, G. L. Trapping of a catalytic HIV reverse transcriptase•template:primer complex through a disulfide bond. Chem. Biol. 7, 355-364 (2000).
    • (2000) Chem. Biol. , vol.7 , pp. 355-364
    • Huang, H.1    Harrison, S.C.2    Verdine, G.L.3
  • 13
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: Implications for drug resistance
    • Huang, H., Chopra, R., Verdine, G. L. & Harrison, S. C. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science 282, 1669-1675 (1998).
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 14
    • 0038018858 scopus 로고    scopus 로고
    • Covalent trapping of protein-DNA complexes
    • Verdine, G. L. & Norman, D. P. Covalent trapping of protein-DNA complexes. Annu. Rev. Biochem. 72, 337-366 (2003).
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 337-366
    • Verdine, G.L.1    Norman, D.P.2
  • 15
    • 1342304229 scopus 로고    scopus 로고
    • Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase
    • Fromme, J. C., Banerjee, A., Huang, S. J. & Verdine, G. L. Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase. Nature 427, 652-656 (2004).
    • (2004) Nature , vol.427 , pp. 652-656
    • Fromme, J.C.1    Banerjee, A.2    Huang, S.J.3    Verdine, G.L.4
  • 16
    • 0036286654 scopus 로고    scopus 로고
    • Free energy simulations come of age: Protein-ligand recognition
    • Simonson, T., Archontis, G. & Karplus, M. Free energy simulations come of age: protein-ligand recognition. Acc. Chem. Res. 35, 430-437 (2002).
    • (2002) Acc. Chem. Res. , vol.35 , pp. 430-437
    • Simonson, T.1    Archontis, G.2    Karplus, M.3
  • 17
    • 2942538198 scopus 로고    scopus 로고
    • Chaperoned alchemical free energy simulations: A general method for QM, MM, and QM/MM potentials
    • Yang, W., Bitetti-Putzer, R. & Karplus, M. Chaperoned alchemical free energy simulations: A general method for QM, MM, and QM/MM potentials. J. Chem. Phys. 120, 9450-9453 (2004).
    • (2004) J. Chem. Phys. , vol.120 , pp. 9450-9453
    • Yang, W.1    Bitetti-Putzer, R.2    Karplus, M.3
  • 19
    • 0031149139 scopus 로고    scopus 로고
    • How do DNA repair proteins locate damaged bases in the genome?
    • Verdine, G. L. & Bruner, S. D. How do DNA repair proteins locate damaged bases in the genome? Chem. Biol. 4, 329-334 (1997).
    • (1997) Chem. Biol. , vol.4 , pp. 329-334
    • Verdine, G.L.1    Bruner, S.D.2
  • 20
    • 0036290411 scopus 로고    scopus 로고
    • Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase
    • Bjoras, M., Seeberg, E., Luna, L., Pearl, L. H. & Barrett, T. E. Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase. J. Mol. Biol. 317, 171-177 (2002).
    • (2002) J. Mol. Biol. , vol.317 , pp. 171-177
    • Bjoras, M.1    Seeberg, E.2    Luna, L.3    Pearl, L.H.4    Barrett, T.E.5
  • 21
    • 0032518911 scopus 로고    scopus 로고
    • Release of normal bases from intact DNA by a native DNA repair enzyme
    • Berdal, K. G., Johansen, R. F. & Seeberg, E. Release of normal bases from intact DNA by a native DNA repair enzyme. EMBO J. 17, 363-367 (1998).
    • (1998) EMBO J. , vol.17 , pp. 363-367
    • Berdal, K.G.1    Johansen, R.F.2    Seeberg, E.3
  • 22
    • 3042686671 scopus 로고    scopus 로고
    • The Escherichia coli 3-methyladenine DNA glycosylase AlkA has a remarkably versatile active site
    • O'Brien, P. J. & Ellenberger, T. The Escherichia coli 3-methyladenine DNA glycosylase AlkA has a remarkably versatile active site. J. Biol. Chem. 279, 26876-26884 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 26876-26884
    • O'Brien, P.J.1    Ellenberger, T.2
  • 23
    • 0025969972 scopus 로고
    • Engineering tethered DNA molecules by the convertible nucleoside approach
    • MacMillan, A. M. & Verdine, G. L. Engineering tethered DNA molecules by the convertible nucleoside approach. Tetrahedron 47, 2603-2616 (1991).
    • (1991) Tetrahedron , vol.47 , pp. 2603-2616
    • MacMillan, A.M.1    Verdine, G.L.2
  • 25
    • 0031076776 scopus 로고    scopus 로고
    • pH-dependence of protein stability: Absolute electrostatic free energy differences between conformations
    • Schaefer, M., Sommer, M. & Karplus, M. pH-dependence of protein stability: absolute electrostatic free energy differences between conformations. J. Phys. Chem. B 101, 1663-1683 (1997).
    • (1997) J. Phys. Chem. B , vol.101 , pp. 1663-1683
    • Schaefer, M.1    Sommer, M.2    Karplus, M.3
  • 26
    • 0035138648 scopus 로고    scopus 로고
    • A QM/MM implementation of the self-consistent charge density functional tight binding (SCC-DFTB) method
    • Cui, Q., Elstner, M., Kaxiras, E., Frauenheim, T. & Karplus, M. A QM/MM implementation of the self-consistent charge density functional tight binding (SCC-DFTB) method. J. Phys. Chem. B 105, 569-585 (2001).
    • (2001) J. Phys. Chem. B , vol.105 , pp. 569-585
    • Cui, Q.1    Elstner, M.2    Kaxiras, E.3    Frauenheim, T.4    Karplus, M.5
  • 27
    • 0035909316 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase acts by substrate autocatalysis
    • Dinner, A. R., Blackburn, G. M. & Karplus, M. Uracil-DNA glycosylase acts by substrate autocatalysis. Nature 413, 752-755 (2001).
    • (2001) Nature , vol.413 , pp. 752-755
    • Dinner, A.R.1    Blackburn, G.M.2    Karplus, M.3
  • 28
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell, A. D. Jr et al. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 102, 3586-3616 (1998).
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell Jr., A.D.1
  • 29
    • 0031561292 scopus 로고    scopus 로고
    • Continuum treatment of long-range interactions in free energy calculations. Application to protein-ligand binding
    • Simonson, T., Archontis, G. & Karplus, M. Continuum treatment of long-range interactions in free energy calculations. Application to protein-ligand binding. J. Phys. Chem. B 101, 8347-8360 (1997).
    • (1997) J. Phys. Chem. B , vol.101 , pp. 8347-8360
    • Simonson, T.1    Archontis, G.2    Karplus, M.3
  • 30
    • 0025743628 scopus 로고
    • Computer simulation and analysis of the reaction pathway of triosephosphate isomerase
    • Bash, P. A. et al. Computer simulation and analysis of the reaction pathway of triosephosphate isomerase. Biochemistry 30, 5826-5832 (1991).
    • (1991) Biochemistry , vol.30 , pp. 5826-5832
    • Bash, P.A.1
  • 31
    • 0027787459 scopus 로고
    • The crystal structure of N4-methylcytosine.guanosine base-pairs in the synthetic hexanucleotide d(CGCGm4CG)
    • Cervi, A. R., Guy, A., Leonard, G. A., Teoule, R. & Hunter, W. N. The crystal structure of N4-methylcytosine.guanosine base-pairs in the synthetic hexanucleotide d(CGCGm4CG). Nucleic Acids Res. 21, 5623-5629 (1993).
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5623-5629
    • Cervi, A.R.1    Guy, A.2    Leonard, G.A.3    Teoule, R.4    Hunter, W.N.5


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