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Volumn 39, Issue 2, 2011, Pages 744-754

DNA intercalation without flipping in the specific ThaI-DNA complex

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CALCIUM ION; CYTOSINE; GLUTAMIC ACID; GUANINE; LYSINE; MAGNESIUM ION; METHIONINE; PROTEIN DERIVATIVE; RESTRICTION ENDONUCLEASE; RESTRICTION ENDONUCLEASE HINCII; RESTRICTION ENDONUCLEASE HINPII; RESTRICTION ENDONUCLEASE THAI; SODIUM ION; TYPE II SITE SPECIFIC DEOXYRIBONUCLEASE; UNCLASSIFIED DRUG;

EID: 79551475839     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq834     Document Type: Article
Times cited : (13)

References (81)
  • 1
    • 46349101158 scopus 로고    scopus 로고
    • Structural and evolutionary classification of Type II restriction enzymes based on theoretical and experimental analyses
    • Orlowski, J. and Bujnicki, J.M. (2008) Structural and evolutionary classification of Type II restriction enzymes based on theoretical and experimental analyses. Nucleic Acids Res., 36, 3552-3569.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3552-3569
    • Orlowski, J.1    Bujnicki, J.M.2
  • 2
    • 0035883723 scopus 로고    scopus 로고
    • Structure and function of type II restriction endonucleases
    • Pingoud, A. and Jeltsch, A. (2001) Structure and function of type II restriction endonucleases. Nucleic Acids Res., 29, 3705-3727.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3705-3727
    • Pingoud, A.1    Jeltsch, A.2
  • 5
    • 4444373591 scopus 로고    scopus 로고
    • An asymmetric complex of restriction endonuclease MspI on its palindromic DNA recognition site
    • Xu, Q.S., Kucera, R.B., Roberts, R.J. and Guo, H.C. (2004) An asymmetric complex of restriction endonuclease MspI on its palindromic DNA recognition site. Structure, 12, 1741-1747.
    • (2004) Structure , vol.12 , pp. 1741-1747
    • Xu, Q.S.1    Kucera, R.B.2    Roberts, R.J.3    Guo, H.C.4
  • 6
    • 0028172810 scopus 로고
    • Five-stranded beta-sheet sandwiched with two alpha-helices: A structural link between restriction endonucleases EcoRI and EcoRV
    • Venclovas, C., Timinskas, A. and Siksnys, V. (1994) Five-stranded beta-sheet sandwiched with two alpha-helices: a structural link between restriction endonucleases EcoRI and EcoRV. Proteins, 20, 279-282.
    • (1994) Proteins , vol.20 , pp. 279-282
    • Venclovas, C.1    Timinskas, A.2    Siksnys, V.3
  • 9
    • 55549123481 scopus 로고    scopus 로고
    • An equivalent metal ion in one- and two-metal-ion catalysis
    • Yang, W. (2008) An equivalent metal ion in one- and two-metal-ion catalysis. Nat. Struct. Mol. Biol., 15, 1228-1231.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1228-1231
    • Yang, W.1
  • 10
    • 77952542578 scopus 로고    scopus 로고
    • Nucleophile activation in PD. . .(D/E)xK metallonucleases: An experimental and computational pK(a) study
    • Xie, F., Briggs, J.M. and Dupureur, C.M. (2010) Nucleophile activation in PD. . .(D/E)xK metallonucleases: an experimental and computational pK(a) study. J. Inorg. Biochem.
    • (2010) J. Inorg. Biochem
    • Xie, F.1    Briggs, J.M.2    Dupureur, C.M.3
  • 11
    • 0037180394 scopus 로고    scopus 로고
    • Catalytic mechanisms of restriction and homing endonucleases
    • Galburt, E.A. and Stoddard, B.L. (2002) Catalytic mechanisms of restriction and homing endonucleases. Biochemistry, 41, 13851-13860.
    • (2002) Biochemistry , vol.41 , pp. 13851-13860
    • Galburt, E.A.1    Stoddard, B.L.2
  • 12
    • 67649888360 scopus 로고    scopus 로고
    • Crystal structure of the beta beta alpha-Me type II restriction endonuclease Hpy99I with target DNA
    • Sokolowska, M., Czapinska, H. and Bochtler, M. (2009) Crystal structure of the beta beta alpha-Me type II restriction endonuclease Hpy99I with target DNA. Nucleic Acids Res., 37, 3799-3810.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3799-3810
    • Sokolowska, M.1    Czapinska, H.2    Bochtler, M.3
  • 15
    • 0035151431 scopus 로고    scopus 로고
    • Grouping together highly diverged PD-(D/E)XK nucleases and identification of novel superfamily members using structure-guided alignment of sequence profiles
    • Bujnicki, J.M. and Rychlewski, L. (2001) Grouping together highly diverged PD-(D/E)XK nucleases and identification of novel superfamily members using structure-guided alignment of sequence profiles. J. Mol. Microbiol. Biotechnol., 3, 69-72.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 69-72
    • Bujnicki, J.M.1    Rychlewski, L.2
  • 16
  • 17
    • 0029048413 scopus 로고
    • Structure of Bam HI endonuclease bound to DNA: Partial folding and unfolding on DNA binding
    • Newman, M., Strzelecka, T., Dorner, L.F., Schildkraut, I. and Aggarwal, A.K. (1995) Structure of Bam HI endonuclease bound to DNA: partial folding and unfolding on DNA binding. Science, 269, 656-663.
    • (1995) Science , vol.269 , pp. 656-663
    • Newman, M.1    Strzelecka, T.2    Dorner, L.F.3    Schildkraut, I.4    Aggarwal, A.K.5
  • 18
    • 0033981010 scopus 로고    scopus 로고
    • Understanding the immutability of restriction enzymes: Crystal structure of BglII and its DNA substrate at 1.5 A resolution
    • Lukacs, C.M., Kucera, R., Schildkraut, I. and Aggarwal, A.K. (2000) Understanding the immutability of restriction enzymes: crystal structure of BglII and its DNA substrate at 1.5 A resolution. Nat. Struct. Biol., 7, 134-140.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 134-140
    • Lukacs, C.M.1    Kucera, R.2    Schildkraut, I.3    Aggarwal, A.K.4
  • 19
    • 41449117713 scopus 로고    scopus 로고
    • Structures of the rare-cutting restriction endonuclease NotI reveal a unique metal binding fold involved in DNA binding
    • Lambert, A.R., Sussman, D., Shen, B., Maunus, R., Nix, J., Samuelson, J., Xu, S.Y. and Stoddard, B.L. (2008) Structures of the rare-cutting restriction endonuclease NotI reveal a unique metal binding fold involved in DNA binding. Structure, 16, 558-569.
    • (2008) Structure , vol.16 , pp. 558-569
    • Lambert, A.R.1    Sussman, D.2    Shen, B.3    Maunus, R.4    Nix, J.5    Samuelson, J.6    Xu, S.Y.7    Stoddard, B.L.8
  • 20
    • 14044252836 scopus 로고    scopus 로고
    • Crystal structures of type II restriction endonuclease EcoO109I and its complex with cognate DNA
    • Hashimoto, H., Shimizu, T., Imasaki, T., Kato, M., Shichijo, N., Kita, K. and Sato, M. (2005) Crystal structures of type II restriction endonuclease EcoO109I and its complex with cognate DNA. J. Biol. Chem., 280, 5605-5610.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5605-5610
    • Hashimoto, H.1    Shimizu, T.2    Imasaki, T.3    Kato, M.4    Shichijo, N.5    Kita, K.6    Sato, M.7
  • 21
    • 0033818703 scopus 로고    scopus 로고
    • Structure of the tetrameric restriction endonuclease NgoMIV in complex with cleaved DNA
    • Deibert, M., Grazulis, S., Sasnauskas, G., Siksnys, V. and Huber, R. (2000) Structure of the tetrameric restriction endonuclease NgoMIV in complex with cleaved DNA. Nat. Struct. Biol., 7, 792-799.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 792-799
    • Deibert, M.1    Grazulis, S.2    Sasnauskas, G.3    Siksnys, V.4    Huber, R.5
  • 23
    • 0029975922 scopus 로고    scopus 로고
    • Probing the indirect readout of the restriction enzyme EcoRV. Mutational analysis of contacts to the DNA backbone
    • Wenz, C., Jeltsch, A. and Pingoud, A. (1996) Probing the indirect readout of the restriction enzyme EcoRV. Mutational analysis of contacts to the DNA backbone. J. Biol. Chem., 271, 5565-5573.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5565-5573
    • Wenz, C.1    Jeltsch, A.2    Pingoud, A.3
  • 25
    • 0032972857 scopus 로고    scopus 로고
    • Structural and energetic origins of indirect readout in site-specific DNA cleavage by a restriction endonuclease
    • Martin, A.M., Sam, M.D., Reich, N.O. and Perona, J.J. (1999) Structural and energetic origins of indirect readout in site-specific DNA cleavage by a restriction endonuclease. Nat. Struct. Biol., 6, 269-277.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 269-277
    • Martin, A.M.1    Sam, M.D.2    Reich, N.O.3    Perona, J.J.4
  • 26
    • 0036143789 scopus 로고    scopus 로고
    • Sequence selectivity and degeneracy of a restriction endonuclease mediated by DNA intercalation
    • Horton, N.C., Dorner, L.F. and Perona, J.J. (2002) Sequence selectivity and degeneracy of a restriction endonuclease mediated by DNA intercalation. Nat. Struct. Biol., 9, 42-47.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 42-47
    • Horton, N.C.1    Dorner, L.F.2    Perona, J.J.3
  • 27
    • 57049101786 scopus 로고    scopus 로고
    • Early interrogation and recognition of DNA sequence by indirect readout
    • Little, E.J., Babic, A.C. and Horton, N.C. (2008) Early interrogation and recognition of DNA sequence by indirect readout. Structure, 16, 1828-1837.
    • (2008) Structure , vol.16 , pp. 1828-1837
    • Little, E.J.1    Babic, A.C.2    Horton, N.C.3
  • 29
    • 33747689885 scopus 로고    scopus 로고
    • Alteration of sequence specificity of the type II restriction endonuclease HincII through an indirect readout mechanism
    • Joshi, H.K., Etzkorn, C., Chatwell, L., Bitinaite, J. and Horton, N.C. (2006) Alteration of sequence specificity of the type II restriction endonuclease HincII through an indirect readout mechanism. J. Biol. Chem., 281, 23852-23869.
    • (2006) J. Biol. Chem. , vol.281 , pp. 23852-23869
    • Joshi, H.K.1    Etzkorn, C.2    Chatwell, L.3    Bitinaite, J.4    Horton, N.C.5
  • 31
    • 71049141657 scopus 로고    scopus 로고
    • Structural mechanisms for the 50-CCWGG sequence recognition by the N- and C-terminal domains of EcoRII
    • Golovenko, D., Manakova, E., Tamulaitiene, G., Grazulis, S. and Siksnys, V. (2009) Structural mechanisms for the 50-CCWGG sequence recognition by the N- and C-terminal domains of EcoRII. Nucleic Acids Res., 37, 6613-6624.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6613-6624
    • Golovenko, D.1    Manakova, E.2    Tamulaitiene, G.3    Grazulis, S.4    Siksnys, V.5
  • 32
    • 0028988416 scopus 로고
    • Mg2+ binding to the active site of EcoRV endonuclease: A crystallographic study of complexes with substrate and product DNA at 2 A resolution
    • Kostrewa, D. and Winkler, F.K. (1995) Mg2+ binding to the active site of EcoRV endonuclease: a crystallographic study of complexes with substrate and product DNA at 2 A resolution. Biochemistry, 34, 683-696.
    • (1995) Biochemistry , vol.34 , pp. 683-696
    • Kostrewa, D.1    Winkler, F.K.2
  • 33
    • 0032502924 scopus 로고    scopus 로고
    • Role of protein-induced bending in the specificity of DNA recognition: Crystal structure of EcoRV endonuclease complexed with d(AAAGAT)+d(ATCTT
    • Horton, N.C. and Perona, J.J. (1998) Role of protein-induced bending in the specificity of DNA recognition: crystal structure of EcoRV endonuclease complexed with d(AAAGAT)+d(ATCTT). J. Mol. Biol., 277, 779-787.
    • (1998) J. Mol. Biol. , vol.277 , pp. 779-787
    • Horton, N.C.1    Perona, J.J.2
  • 35
    • 0017819050 scopus 로고
    • A restriction enzyme Tha i from the thermophilic mycoplasma Thermoplasma acidophilum
    • McConnell, D.J., Searcy, D.G. and Sutcliffe, J.G. (1978) A restriction enzyme Tha I from the thermophilic mycoplasma Thermoplasma acidophilum. Nucleic Acids Res., 5, 1729-1739.
    • (1978) Nucleic Acids Res. , vol.5 , pp. 1729-1739
    • McConnell, D.J.1    Searcy, D.G.2    Sutcliffe, J.G.3
  • 37
    • 0021761269 scopus 로고
    • Methylation of either cytosine in the recognition sequence CGCG inhibits ThaI cleavage of DNA
    • Strobl, J.S. and Thompson, E.B. (1984) Methylation of either cytosine in the recognition sequence CGCG inhibits ThaI cleavage of DNA. Nucleic Acids Res., 12, 8073-8083.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 8073-8083
    • Strobl, J.S.1    Thompson, E.B.2
  • 38
    • 0030046809 scopus 로고    scopus 로고
    • Intercalation, DNA kinking, and the control of transcription
    • Werner, M.H., Gronenborn, A.M. and Clore, G.M. (1996) Intercalation, DNA kinking, and the control of transcription. Science, 271, 778-784.
    • (1996) Science , vol.271 , pp. 778-784
    • Werner, M.H.1    Gronenborn, A.M.2    Clore, G.M.3
  • 41
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. (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
  • 43
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris, R.J., Perrakis, A. and Lamzin, V.S. (2003) ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol., 374, 229-244.
    • (2003) Methods Enzymol. , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 44
    • 50349085962 scopus 로고    scopus 로고
    • 3DNA: A versatile, integrated software system for the analysis, rebuilding and visualization of three-dimensional nucleic-acid structures
    • Lu, X.J. and Olson, W.K. (2008) 3DNA: a versatile, integrated software system for the analysis, rebuilding and visualization of three-dimensional nucleic-acid structures. Nat. Protoc., 3, 1213-1227.
    • (2008) Nat. Protoc. , vol.3 , pp. 1213-1227
    • Lu, X.J.1    Olson, W.K.2
  • 47
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brunger, A.T. (2007) Version 1.2 of the crystallography and NMR system. Nat. Protoc., 2, 2728-2733.
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 48
    • 34047245428 scopus 로고    scopus 로고
    • A sliding restriction enzyme pauses
    • Pingoud, A. and Wende, W. (2007) A sliding restriction enzyme pauses. Structure, 15, 391-393.
    • (2007) Structure , vol.15 , pp. 391-393
    • Pingoud, A.1    Wende, W.2
  • 49
    • 0034885432 scopus 로고    scopus 로고
    • Structure of NaeI-DNA complex reveals dual-mode DNA recognition and complete dimer rearrangement
    • Huai, Q., Colandene, J.D., Topal, M.D. and Ke, H. (2001) Structure of NaeI-DNA complex reveals dual-mode DNA recognition and complete dimer rearrangement. Nat. Struct. Biol., 8, 665-669.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 665-669
    • Huai, Q.1    Colandene, J.D.2    Topal, M.D.3    Ke, H.4
  • 50
    • 0034660061 scopus 로고    scopus 로고
    • Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease and topoisomerase
    • Huai, Q., Colandene, J.D., Chen, Y., Luo, F., Zhao, Y., Topal, M.D. and Ke, H. (2000) Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease and topoisomerase. EMBO J., 19, 3110-3118.
    • (2000) EMBO J. , vol.19 , pp. 3110-3118
    • Huai, Q.1    Colandene, J.D.2    Chen, Y.3    Luo, F.4    Zhao, Y.5    Topal, M.D.6    Ke, H.7
  • 51
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L. and Rosenstrom, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res., 38(Suppl.), W545-W549.
    • (2010) Nucleic Acids Res. , vol.38 , Issue.SUPPL.
    • Holm, L.1    Rosenstrom, P.2
  • 53
    • 0035906281 scopus 로고    scopus 로고
    • Identification of a PD-(D/ E)XK-like domain with a novel configuration of the endonuclease active site in the methyl-directed restriction enzyme Mrr and its homologs
    • Bujnicki, J.M. and Rychlewski, L. (2001) Identification of a PD-(D/ E)XK-like domain with a novel configuration of the endonuclease active site in the methyl-directed restriction enzyme Mrr and its homologs. Gene, 267, 183-191.
    • (2001) Gene , vol.267 , pp. 183-191
    • Bujnicki, J.M.1    Rychlewski, L.2
  • 54
    • 0032486108 scopus 로고    scopus 로고
    • Structure-based redesign of the catalytic/metal binding site of Cfr10I restriction endonuclease reveals importance of spatial rather than sequence conservation of active centre residues
    • Skirgaila, R., Grazulis, S., Bozic, D., Huber, R. and Siksnys, V. (1998) Structure-based redesign of the catalytic/metal binding site of Cfr10I restriction endonuclease reveals importance of spatial rather than sequence conservation of active centre residues. J. Mol. Biol., 279, 473-481.
    • (1998) J. Mol. Biol. , vol.279 , pp. 473-481
    • Skirgaila, R.1    Grazulis, S.2    Bozic, D.3    Huber, R.4    Siksnys, V.5
  • 55
    • 0032506110 scopus 로고    scopus 로고
    • Metal ion-mediated substrate-assisted catalysis in type II restriction endonucleases
    • Horton, N.C., Newberry, K.J. and Perona, J.J. (1998) Metal ion-mediated substrate-assisted catalysis in type II restriction endonucleases. Proc. Natl Acad. Sci. USA, 95, 13489-13494.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13489-13494
    • Horton, N.C.1    Newberry, K.J.2    Perona, J.J.3
  • 56
    • 70349784082 scopus 로고    scopus 로고
    • Catalytic mechanism of DNA backbone cleavage by the restriction enzyme EcoRV: A quantum mechanical/molecular mechanical analysis
    • Imhof, P., Fischer, S. and Smith, J.C. (2009) Catalytic mechanism of DNA backbone cleavage by the restriction enzyme EcoRV: a quantum mechanical/molecular mechanical analysis. Biochemistry, 48, 9061-9075.
    • (2009) Biochemistry , vol.48 , pp. 9061-9075
    • Imhof, P.1    Fischer, S.2    Smith, J.C.3
  • 57
    • 33846165757 scopus 로고    scopus 로고
    • Metal-binding sites at the active site of restriction endonuclease BamHI can conform to a one-ion mechanism
    • Mones, L., Simon, I. and Fuxreiter, M. (2007) Metal-binding sites at the active site of restriction endonuclease BamHI can conform to a one-ion mechanism. Biol. Chem., 388, 73-78.
    • (2007) Biol. Chem. , vol.388 , pp. 73-78
    • Mones, L.1    Simon, I.2    Fuxreiter, M.3
  • 58
    • 0029075461 scopus 로고
    • Molecular basis of human 46X, y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex
    • Werner, M.H., Huth, J.R., Gronenborn, A.M. and Clore, G.M. (1995) Molecular basis of human 46X, Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell, 81, 705-714.
    • (1995) Cell , vol.81 , pp. 705-714
    • Werner, M.H.1    Huth, J.R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 59
    • 0030451819 scopus 로고    scopus 로고
    • Crystal structure of an IHF-DNA complex: A protein-induced DNA U-turn
    • Rice, P.A., Yang, S., Mizuuchi, K. and Nash, H.A. (1996) Crystal structure of an IHF-DNA complex: a protein-induced DNA U-turn. Cell, 87, 1295-1306.
    • (1996) Cell , vol.87 , pp. 1295-1306
    • Rice, P.A.1    Yang, S.2    Mizuuchi, K.3    Nash, H.A.4
  • 60
    • 0041312645 scopus 로고    scopus 로고
    • Flexible DNA bending in HU-DNA cocrystal structures
    • Swinger, K.K., Lemberg, K.M., Zhang, Y. and Rice, P.A. (2003) Flexible DNA bending in HU-DNA cocrystal structures. EMBO J., 22, 3749-3760.
    • (2003) EMBO J. , vol.22 , pp. 3749-3760
    • Swinger, K.K.1    Lemberg, K.M.2    Zhang, Y.3    Rice, P.A.4
  • 61
    • 33846954751 scopus 로고    scopus 로고
    • Shaping the Borrelia burgdorferi genome: Crystal structure and binding properties of the DNA-bending protein Hbb
    • Mouw, K.W. and Rice, P.A. (2007) Shaping the Borrelia burgdorferi genome: crystal structure and binding properties of the DNA-bending protein Hbb. Mol. Microbiol., 63, 1319-1330.
    • (2007) Mol. Microbiol. , vol.63 , pp. 1319-1330
    • Mouw, K.W.1    Rice, P.A.2
  • 62
    • 0028173030 scopus 로고
    • Crystal structure of LacI member, PurR, bound to DNA: Minor groove binding by alpha helices
    • Schumacher, M.A., Choi, K.Y., Zalkin, H. and Brennan, R.G. (1994) Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices. Science, 266, 763-770.
    • (1994) Science , vol.266 , pp. 763-770
    • Schumacher, M.A.1    Choi, K.Y.2    Zalkin, H.3    Brennan, R.G.4
  • 64
    • 0042161878 scopus 로고    scopus 로고
    • Crystal structure of a POU/HMG/DNA ternary complex suggests differential assembly of Oct4 and Sox2 on two enhancers
    • Remenyi, A., Lins, K., Nissen, L.J., Reinbold, R., Scholer, H.R. and Wilmanns, M. (2003) Crystal structure of a POU/HMG/DNA ternary complex suggests differential assembly of Oct4 and Sox2 on two enhancers. Genes Dev., 17, 2048-2059.
    • (2003) Genes Dev. , vol.17 , pp. 2048-2059
    • Remenyi, A.1    Lins, K.2    Nissen, L.J.3    Reinbold, R.4    Scholer, H.R.5    Wilmanns, M.6
  • 65
    • 64649095458 scopus 로고    scopus 로고
    • The structure of Sox17 bound to DNA reveals a conserved bending topology but selective protein interaction platforms
    • Palasingam, P., Jauch, R., Ng, C.K. and Kolatkar, P.R. (2009) The structure of Sox17 bound to DNA reveals a conserved bending topology but selective protein interaction platforms. J. Mol. Biol., 388, 619-630.
    • (2009) J. Mol. Biol. , vol.388 , pp. 619-630
    • Palasingam, P.1    Jauch, R.2    Ng, C.K.3    Kolatkar, P.R.4
  • 66
    • 0036404246 scopus 로고    scopus 로고
    • The S. cerevisiae architectural HMGB protein NHP6A complexed with DNA: DNA and protein conformational changes upon binding
    • Masse, J.E., Wong, B., Yen, Y.M., Allain, F.H., Johnson, R.C. and Feigon, J. (2002) The S. cerevisiae architectural HMGB protein NHP6A complexed with DNA: DNA and protein conformational changes upon binding. J. Mol. Biol., 323, 263-284.
    • (2002) J. Mol. Biol. , vol.323 , pp. 263-284
    • Masse, J.E.1    Wong, B.2    Yen, Y.M.3    Allain, F.H.4    Johnson, R.C.5    Feigon, J.6
  • 67
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATA-box complex
    • Kim, Y., Geiger, J.H., Hahn, S. and Sigler, P.B. (1993) Crystal structure of a yeast TBP/TATA-box complex. Nature, 365, 512-520.
    • (1993) Nature , vol.365 , pp. 512-520
    • Kim, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 68
    • 0027483012 scopus 로고
    • Co-crystal structure of TBP recognizing the minor groove of a TATA element
    • Kim, J.L., Nikolov, D.B. and Burley, S.K. (1993) Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature, 365, 520-527.
    • (1993) Nature , vol.365 , pp. 520-527
    • Kim, J.L.1    Nikolov, D.B.2    Burley, S.K.3
  • 69
    • 0028010888 scopus 로고
    • HhaI methyltransferase flips its target base out of the DNA helix
    • Klimasauskas, S., Kumar, S., Roberts, R.J. and Cheng, X. (1994) HhaI methyltransferase flips its target base out of the DNA helix. Cell, 76, 357-369.
    • (1994) Cell , vol.76 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 70
    • 0033544707 scopus 로고    scopus 로고
    • Recognition of a TG mismatch: The crystal structure of very short patch repair endonuclease in complex with a DNA duplex
    • Tsutakawa, S.E., Jingami, H. and Morikawa, K. (1999) Recognition of a TG mismatch: the crystal structure of very short patch repair endonuclease in complex with a DNA duplex. Cell, 99, 615-623.
    • (1999) Cell , vol.99 , pp. 615-623
    • Tsutakawa, S.E.1    Jingami, H.2    Morikawa, K.3
  • 71
    • 0034641938 scopus 로고    scopus 로고
    • Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA
    • Obmolova, G., Ban, C., Hsieh, P. and Yang, W. (2000) Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA. Nature, 407, 703-710.
    • (2000) Nature , vol.407 , pp. 703-710
    • Obmolova, G.1    Ban, C.2    Hsieh, P.3    Yang, W.4
  • 72
    • 0034641947 scopus 로고    scopus 로고
    • The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch
    • Lamers, M.H., Perrakis, A., Enzlin, J.H., Winterwerp, H.H., de Wind, N. and Sixma, T.K. (2000) The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch. Nature, 407, 711-717.
    • (2000) Nature , vol.407 , pp. 711-717
    • Lamers, M.H.1    Perrakis, A.2    Enzlin, J.H.3    Winterwerp, H.H.4    De Wind, N.5    Sixma, T.K.6
  • 73
    • 33644511436 scopus 로고    scopus 로고
    • Structure of a DNA glycosylase searching for lesions
    • Banerjee, A., Santos, W.L. and Verdine, G.L. (2006) Structure of a DNA glycosylase searching for lesions. Science, 311, 1153-1157.
    • (2006) Science , vol.311 , pp. 1153-1157
    • Banerjee, A.1    Santos, W.L.2    Verdine, G.L.3
  • 75
    • 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. and Verdine, G.L. (2004) Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase. Nature, 427, 652-656.
    • (2004) Nature , vol.427 , pp. 652-656
    • Fromme, J.C.1    Banerjee, A.2    Huang, S.J.3    Verdine, G.L.4
  • 76
    • 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. (1996) A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Nature, 384, 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
  • 77
    • 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. (1998) Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell, 92, 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
  • 78
    • 42549128712 scopus 로고    scopus 로고
    • Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA
    • Yang, C.G., Yi, C., Duguid, E.M., Sullivan, C.T., Jian, X., Rice, P.A. and He, C. (2008) Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA. Nature, 452, 961-965.
    • (2008) Nature , vol.452 , pp. 961-965
    • Yang, C.G.1    Yi, C.2    Duguid, E.M.3    Sullivan, C.T.4    Jian, X.5    Rice, P.A.6    He, C.7
  • 80
    • 34948892722 scopus 로고    scopus 로고
    • Recognition of DNA damage by the Rad4 nucleotide excision repair protein
    • Min, J.H. and Pavletich, N.P. (2007) Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature, 449, 570-575.
    • (2007) Nature , vol.449 , pp. 570-575
    • Min, J.H.1    Pavletich, N.P.2
  • 81
    • 10044280323 scopus 로고    scopus 로고
    • Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair
    • Mees, A., Klar, T., Gnau, P., Hennecke, U., Eker, A.P., Carell, T. and Essen, L.O. (2004) Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair. Science, 306, 1789-1793.
    • (2004) Science , vol.306 , pp. 1789-1793
    • Mees, A.1    Klar, T.2    Gnau, P.3    Hennecke, U.4    Eker, A.P.5    Carell, T.6    Essen, L.O.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.