메뉴 건너뛰기




Volumn 373, Issue 4, 2007, Pages 839-850

Crystal Structure of Family 5 Uracil-DNA Glycosylase Bound to DNA

Author keywords

crystal structure; DNA complex; DNA repair; family 5 UDG; uracil DNA glycosylase

Indexed keywords

ASPARAGINE; DNA; LIGAND; URACIL DNA GLYCOSIDASE; WATER;

EID: 34848920082     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.08.022     Document Type: Article
Times cited : (41)

References (32)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T. Instability and decay of the primary structure of DNA. Nature 362 (1993) 709-715
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 2
    • 0028358421 scopus 로고
    • The rate of hydrolytic deamination of 5-methylcytosine in double-stranded DNA
    • Shen J.-C., Rideout W.M.I., and Jones P.A. The rate of hydrolytic deamination of 5-methylcytosine in double-stranded DNA. Nucleic Acids Res. 22 (1994) 972-997
    • (1994) Nucleic Acids Res. , vol.22 , pp. 972-997
    • Shen, J.-C.1    Rideout, W.M.I.2    Jones, P.A.3
  • 4
    • 0034734380 scopus 로고    scopus 로고
    • Lessons learned from structural results on uracil-DNA glycosylase
    • Parikh S.S., Putnam C.D., and Tainer J.A. Lessons learned from structural results on uracil-DNA glycosylase. Mutat. Res. 460 (2000) 183-199
    • (2000) Mutat. Res. , vol.460 , pp. 183-199
    • Parikh, S.S.1    Putnam, C.D.2    Tainer, J.A.3
  • 5
    • 0035111895 scopus 로고    scopus 로고
    • Recent progress in the biology, chemistry and structural biology of DNA glycosylases
    • Scharer O.D., and Jiricny J. Recent progress in the biology, chemistry and structural biology of DNA glycosylases. Bioessays 23 (2001) 270-281
    • (2001) Bioessays , vol.23 , pp. 270-281
    • Scharer, O.D.1    Jiricny, J.2
  • 6
    • 0034734383 scopus 로고    scopus 로고
    • Structure and function in the uracil-DNA glycosylase superfamily
    • Pearl L.H. Structure and function in the uracil-DNA glycosylase superfamily. Mutat. Res. 460 (2000) 165-181
    • (2000) Mutat. Res. , vol.460 , pp. 165-181
    • Pearl, L.H.1
  • 7
    • 0033120232 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited
    • Xiao G., Xiao G., Tordova M., Jagadeesh J., Drohat A.C., Stivers J.T., and Gilliland G.L. Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited. Proteins 35 (1999) 13-24
    • (1999) Proteins , vol.35 , pp. 13-24
    • Xiao, G.1    Xiao, G.2    Tordova, M.3    Jagadeesh, J.4    Drohat, A.C.5    Stivers, J.T.6    Gilliland, G.L.7
  • 8
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis
    • Mol C.D., Arvai A.S., Slupphaug G., Kavli B., Alseth I., Krokan H.E., and Tainer J.A. Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. Cell 80 (1995) 869-878
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavli, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 9
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracil-DNA glycosylase
    • Savva R., McAuley-Hecht K., Brown T., and Pearl L. The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature 373 (1995) 487-493
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R.1    McAuley-Hecht, K.2    Brown, T.3    Pearl, L.4
  • 10
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
    • Slupphaug G., Mol C.D., Kavli B., Arvai A.S., Krokan H.E., and Tainer J.A. A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Nature 384 (1996) 87-92
    • (1996) Nature , vol.384 , pp. 87-92
    • Slupphaug, G.1    Mol, C.D.2    Kavli, B.3    Arvai, A.S.4    Krokan, H.E.5    Tainer, J.A.6
  • 11
    • 0032498302 scopus 로고    scopus 로고
    • Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions
    • Barrett T.E., Savva R., Panayotou G., Barlow T., Brown T., Jiricny J., and Pearl L.H. Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 92 (1998) 117-129
    • (1998) Cell , vol.92 , pp. 117-129
    • Barrett, T.E.1    Savva, R.2    Panayotou, G.3    Barlow, T.4    Brown, T.5    Jiricny, J.6    Pearl, L.H.7
  • 12
    • 0033602148 scopus 로고    scopus 로고
    • Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors
    • Haushalter K.A., Todd Stukenberg M.W., Kirschner M.W., and Verdine G.L. Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors. Curr. Biol. 9 (1999) 174-185
    • (1999) Curr. Biol. , vol.9 , pp. 174-185
    • Haushalter, K.A.1    Todd Stukenberg, M.W.2    Kirschner, M.W.3    Verdine, G.L.4
  • 13
    • 0037052965 scopus 로고    scopus 로고
    • A novel type of uracil-DNA glycosylase mediating repair of hydrolytic DNA damage in the extremely thermophilic eubacterium Thermus thermophilus
    • Starkuviene V., and Fritz H.J. A novel type of uracil-DNA glycosylase mediating repair of hydrolytic DNA damage in the extremely thermophilic eubacterium Thermus thermophilus. Nucleic Acids Res. 30 (2002) 2097-2102
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2097-2102
    • Starkuviene, V.1    Fritz, H.J.2
  • 16
    • 0038771139 scopus 로고    scopus 로고
    • Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1
    • Wibley J.E., Waters T.R., Haushalter K., Verdine G.L., and Pearl L.H. Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1. Mol. Cell 11 (2003) 1647-1659
    • (2003) Mol. Cell , vol.11 , pp. 1647-1659
    • Wibley, J.E.1    Waters, T.R.2    Haushalter, K.3    Verdine, G.L.4    Pearl, L.H.5
  • 17
    • 0037125932 scopus 로고    scopus 로고
    • Mutational analysis of the base-flipping mechanism of uracil DNA glycosylase
    • Jiang Y.L., and Stivers J.T. Mutational analysis of the base-flipping mechanism of uracil DNA glycosylase. Biochemistry 41 (2002) 11236-11247
    • (2002) Biochemistry , vol.41 , pp. 11236-11247
    • Jiang, Y.L.1    Stivers, J.T.2
  • 18
    • 0034625082 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects
    • Parikh S.S., Walcher G., Jones G.D., Slupphaug G., Krokan H.E., Blackburn G.M., and Tainer J.A. Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects. Proc. Natl Acad. Sci. USA 97 (2000) 5083-5088
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5083-5088
    • Parikh, S.S.1    Walcher, G.2    Jones, G.D.3    Slupphaug, G.4    Krokan, H.E.5    Blackburn, G.M.6    Tainer, J.A.7
  • 19
    • 0037124349 scopus 로고    scopus 로고
    • A novel uracil-DNA glycosylase with broad substrate specificity and an unusual active site
    • Sartori A.A., Fitz-Gibbon S., Yang H., Miller J.H., and Jiricny J. A novel uracil-DNA glycosylase with broad substrate specificity and an unusual active site. EMBO J. 21 (2002) 3182-3191
    • (2002) EMBO J. , vol.21 , pp. 3182-3191
    • Sartori, A.A.1    Fitz-Gibbon, S.2    Yang, H.3    Miller, J.H.4    Jiricny, J.5
  • 20
    • 0032519382 scopus 로고    scopus 로고
    • Thermostable repair enzyme for oxidative DNA damage from extremely thermophilic bacterium, Thermus thermophilus HB8
    • Mikawa T., Kato R., Sugahara M., and Kuramitsu S. Thermostable repair enzyme for oxidative DNA damage from extremely thermophilic bacterium, Thermus thermophilus HB8. Nucleic Acids Res. 26 (1998) 903-910
    • (1998) Nucleic Acids Res. , vol.26 , pp. 903-910
    • Mikawa, T.1    Kato, R.2    Sugahara, M.3    Kuramitsu, S.4
  • 22
    • 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., and Verdine G.L. Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature 403 (2000) 859-866
    • (2000) Nature , vol.403 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.2    Verdine, G.L.3
  • 23
    • 0034651873 scopus 로고    scopus 로고
    • DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA
    • Hollis T., Ichikawa Y., and Ellenberger T. DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA. EMBO J. 19 (2000) 758-766
    • (2000) EMBO J. , vol.19 , pp. 758-766
    • Hollis, T.1    Ichikawa, Y.2    Ellenberger, T.3
  • 24
    • 21644479309 scopus 로고    scopus 로고
    • Molecular mechanism of the Thermus thermophilus ADP-ribose pyrophosphatase from mutational and kinetic studies
    • Ooga T., Yoshiba S., Nakagawa N., Kuramitsu S., and Masui R. Molecular mechanism of the Thermus thermophilus ADP-ribose pyrophosphatase from mutational and kinetic studies. Biochemistry 44 (2006) 9320-9329
    • (2006) Biochemistry , vol.44 , pp. 9320-9329
    • Ooga, T.1    Yoshiba, S.2    Nakagawa, N.3    Kuramitsu, S.4    Masui, R.5
  • 25
    • 0022273106 scopus 로고
    • 1H-15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type
    • LeMaster D.M., and Richards F.M. 1H-15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type. Biochemistry 24 (1985) 7263-7268
    • (1985) Biochemistry , vol.24 , pp. 7263-7268
    • LeMaster, D.M.1    Richards, F.M.2
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 32
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., and Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr., Sect. D: Biol. Crystallogr. 60 (2004) 2256-2268
    • (2004) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.