메뉴 건너뛰기




Volumn 19, Issue 5, 2000, Pages 1119-1129

Crystal structure of NAD+-dependent DNA ligase: Modular architecture and functional implications

Author keywords

DNA ligase; Helix hairpin helix motif; Nucleotidyl transferase; Oligomer binding fold; Zinc finger motif

Indexed keywords

BACTERIAL ENZYME; DNA BINDING PROTEIN; DOUBLE STRANDED DNA; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; ZINC FINGER PROTEIN;

EID: 0034161570     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.5.1119     Document Type: Article
Times cited : (163)

References (73)
  • 1
    • 0033574503 scopus 로고    scopus 로고
    • Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches
    • Aravind, L. and Koonin, E.V. (1999) Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. J. Mol. Biol., 287, 1023-1040.
    • (1999) J. Mol. Biol. , vol.287 , pp. 1023-1040
    • Aravind, L.1    Koonin, E.V.2
  • 2
    • 0033105094 scopus 로고    scopus 로고
    • Conserved domains in DNA repair proteins and evolution of repair systems
    • Aravind, L., Walker, D.R. and Koonin, E.V. (1999) Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Res., 27, 1223-1242.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1223-1242
    • Aravind, L.1    Walker, D.R.2    Koonin, E.V.3
  • 3
    • 0026056970 scopus 로고
    • Genetic disease detection and DNA amplification using cloned thermostable ligase
    • Barany, F. (1991) Genetic disease detection and DNA amplification using cloned thermostable ligase. Proc. Natl Acad. Sci. USA, 88, 189-193.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 189-193
    • Barany, F.1
  • 4
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
    • Bochkarev, A., Pfuetzner, R.A., Edwards, A.M. and Frappier, L. (1997) Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature, 385, 176-181.
    • (1997) Nature , vol.385 , pp. 176-181
    • Bochkarev, A.1    Pfuetzner, R.A.2    Edwards, A.M.3    Frappier, L.4
  • 5
    • 0033575671 scopus 로고    scopus 로고
    • The crystal structure of the complex of replication protein a subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding
    • Bochkarev, A., Bochkareva, E., Frappier, L. and Edwards, A.M. (1999) The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding. EMBO J., 18, 4498-4504.
    • (1999) EMBO J. , vol.18 , pp. 4498-4504
    • Bochkarev, A.1    Bochkareva, E.2    Frappier, L.3    Edwards, A.M.4
  • 6
    • 0031046294 scopus 로고    scopus 로고
    • A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins
    • Bork, P., Hofmann, K., Bucher, P, Neuwald, A.F., Altschul, S.F. and Koonin, E.V. (1997) A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins. FASEB J., 11, 68-76.
    • (1997) FASEB J. , vol.11 , pp. 68-76
    • Bork, P.1    Hofmann, K.2    Bucher, P.3    Neuwald, A.F.4    Altschul, S.F.5    Koonin, E.V.6
  • 8
    • 0026597444 scopus 로고
    • The free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992b) 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
    • Brünger, A.T.1
  • 9
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. (1998) Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D, 54, 905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 10
    • 0031471204 scopus 로고    scopus 로고
    • The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold
    • Bycroft, M., Hubbard, T.J.P., Proctor, M., Freund, S.M.V. and Murzin, A.G. (1997) The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell, 88, 235-242.
    • (1997) Cell , vol.88 , pp. 235-242
    • Bycroft, M.1    Hubbard, T.J.P.2    Proctor, M.3    Freund, S.M.V.4    Murzin, A.G.5
  • 11
    • 0031031787 scopus 로고    scopus 로고
    • From BRCA1 to RAP1: A widespread BRCT module closely associated with DNA repair
    • Callebaut, I. and Mornon, J.P. (1997) From BRCA1 to RAP1: a widespread BRCT module closely associated with DNA repair. FEBS Lett., 400, 25-30.
    • (1997) FEBS Lett. , vol.400 , pp. 25-30
    • Callebaut, I.1    Mornon, J.P.2
  • 12
    • 0028103275 scopus 로고
    • Collaborative computational project number 4. The CCP4 suite: Programs for protein crystallography
    • (1994) Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D, 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 13
    • 0029166107 scopus 로고
    • Mammalian DNA ligase III: Molecular cloning, chromosomal localization, and expression in spermatocytes undergoing meiotic recombination
    • Chen, J., Tomkinson, A.E., Ramos, W., Mackey, Z.B., Danehower, S., Walter, C.A., Schultz, R.A., Besterman, J.M. and Husain, I. (1995) Mammalian DNA ligase III: molecular cloning, chromosomal localization, and expression in spermatocytes undergoing meiotic recombination. Mol. Cell. Biol., 15, 5412-5422.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5412-5422
    • Chen, J.1    Tomkinson, A.E.2    Ramos, W.3    Mackey, Z.B.4    Danehower, S.5    Walter, C.A.6    Schultz, R.A.7    Besterman, J.M.8    Husain, I.9
  • 14
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de la Fortelle, E. and Bricogne, G. (1997) Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol., 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 15
    • 0029929070 scopus 로고    scopus 로고
    • The helix-hairpin-helix DNA-binding motif: A structural basis for non-sequence-specific recognition of DNA
    • Doherty, A.J., Serpell, L.C. and Ponting, C.P. (1996) The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res., 24, 2488-2497.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2488-2497
    • Doherty, A.J.1    Serpell, L.C.2    Ponting, C.P.3
  • 16
    • 0033556127 scopus 로고    scopus 로고
    • RNA binding strategies of ribosomal proteins
    • Draper, D.E. and Reynaldo, L.P. (1999) RNA binding strategies of ribosomal proteins. Nucleic Acids Res., 27, 381-388.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 381-388
    • Draper, D.E.1    Reynaldo, L.P.2
  • 17
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., Lesk, A.M. and Chothia, C. (1994) Structural mechanisms for domain movements in proteins. Biochemistry, 33, 6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 18
    • 0029010368 scopus 로고
    • The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex
    • Gewirth, D.T. and Sigler, P.B. (1995) The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex. Nature Struct. Biol., 2, 386-394.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 386-394
    • Gewirth, D.T.1    Sigler, P.B.2
  • 20
  • 21
    • 0032539677 scopus 로고    scopus 로고
    • Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping
    • Håkansson, K. and Wigley, D.B. (1998) Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping. Proc. Natl Acad. Sci. USA, 95, 1505-1510.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1505-1510
    • Håkansson, K.1    Wigley, D.B.2
  • 22
    • 0038228666 scopus 로고    scopus 로고
    • X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes
    • Håkansson, K., Doherty, A.J., Shuman, S. and Wigley, D.B. (1997) X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes. Cell, 89, 545-553.
    • (1997) Cell , vol.89 , pp. 545-553
    • Håkansson, K.1    Doherty, A.J.2    Shuman, S.3    Wigley, D.B.4
  • 23
    • 0032431057 scopus 로고    scopus 로고
    • Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA
    • Horvath, M.P., Schweiker, V.L., Bevilacqua, J.M., Ruggles, J.A. and Schultz, S.C. (1998) Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA. Cell, 95, 963-974.
    • (1998) Cell , vol.95 , pp. 963-974
    • Horvath, M.P.1    Schweiker, V.L.2    Bevilacqua, J.M.3    Ruggles, J.A.4    Schultz, S.C.5
  • 24
    • 0029915450 scopus 로고    scopus 로고
    • Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectroscopy
    • Jaishree, T.N., Ramakrishnan, V. and White, S.W. (1996) Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectroscopy. Biochemistry, 35, 2845-2853.
    • (1996) Biochemistry , vol.35 , pp. 2845-2853
    • Jaishree, T.N.1    Ramakrishnan, V.2    White, S.W.3
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0032584830 scopus 로고    scopus 로고
    • Cloning, nucleotide sequence, and expression of the DNA ligase-encoding gene from Thermus filiformis
    • Kim, H.-K. and Kwon, S.-T. (1998) Cloning, nucleotide sequence, and expression of the DNA ligase-encoding gene from Thermus filiformis. Mol. Cell, 8, 438-443.
    • (1998) Mol. Cell , vol.8 , pp. 438-443
    • Kim, H.-K.1    Kwon, S.-T.2
  • 27
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
    • Kjeldgaard, M., Nissen, P., Thirup, S. and Nyborg, J. (1993) The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure, 1, 35-50.
    • (1993) Structure , vol.1 , pp. 35-50
    • Kjeldgaard, M.1    Nissen, P.2    Thirup, S.3    Nyborg, J.4
  • 28
    • 0033613813 scopus 로고    scopus 로고
    • Recognition of spatial motifs in protein structures
    • Kleywegt, G.J. (1999) Recognition of spatial motifs in protein structures. J. Mol. Biol., 285, 1887-1897.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1887-1897
    • Kleywegt, G.J.1
  • 29
  • 30
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E.coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev, S., Hsieh, J., Gauss, G.H., Lohman, T.M. and Waksman, G. (1997) Major domain swiveling revealed by the crystal structures of complexes of E.coli Rep helicase bound to single-stranded DNA and ADP. Cell, 90, 635-647.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 31
    • 0026244229 scopus 로고
    • MOLSCRIPT; a program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT; a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 33
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 35
    • 0016273515 scopus 로고
    • DNA ligase: Structure, mechanism, and function
    • Lehman, I.R. (1974) DNA ligase: structure, mechanism, and function. Science, 186, 790-797.
    • (1974) Science , vol.186 , pp. 790-797
    • Lehman, I.R.1
  • 36
    • 0030692134 scopus 로고    scopus 로고
    • An interaction between DNA ligase I and proliferating cell nuclear antigen: Implications for Okazaki fragment synthesis and joining
    • Levin, D.S., Bai, W., Yao, N., O'Donnell, M. and Tomkinson, A.E. (1997) An interaction between DNA ligase I and proliferating cell nuclear antigen: implications for Okazaki fragment synthesis and joining. Proc. Natl Acad. Sci. USA, 94, 12863-12868.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12863-12868
    • Levin, D.S.1    Bai, W.2    Yao, N.3    O'Donnell, M.4    Tomkinson, A.E.5
  • 37
    • 0028115776 scopus 로고
    • Three-dimensional structure of the 67K N-terminal fragment of E.coli DNA topoisomerase I
    • Lima, C.D., Wang, J.C. and Mondragón, A. (1994) Three-dimensional structure of the 67K N-terminal fragment of E.coli DNA topoisomerase I. Nature, 367, 138-146.
    • (1994) Nature , vol.367 , pp. 138-146
    • Lima, C.D.1    Wang, J.C.2    Mondragón, A.3
  • 39
    • 0029744212 scopus 로고    scopus 로고
    • Identification of essential residues in Thermus thermophilus DNA ligase
    • Luo, J. and Barany, F. (1996) Identification of essential residues in Thermus thermophilus DNA ligase. Nucleic Acids Res., 24, 3079-3085.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3079-3085
    • Luo, J.1    Barany, F.2
  • 40
    • 0029776838 scopus 로고    scopus 로고
    • Improving the fidelity of Thermus thermophilus DNA ligase
    • Luo, J., Bergstrom, D.E. and Barany, F. (1996) Improving the fidelity of Thermus thermophilus DNA ligase. Nucleic Acids Res., 24, 3071-3078.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3071-3078
    • Luo, J.1    Bergstrom, D.E.2    Barany, F.3
  • 41
  • 42
    • 0033618289 scopus 로고    scopus 로고
    • DNA ligase III is recruited to DNA strand breaks by a zinc finger motif homologous to that of poly(ADP-ribose) polymerase. Identification of two functionally distinct DNA binding regions within DNA ligase III
    • Mackey, Z.B., Niedergang, C., Murcia, J.M., Leppard, J., Au, K., Chen, J., de Murcia, G. and Tomkinson, A.E. (1999) DNA ligase III is recruited to DNA strand breaks by a zinc finger motif homologous to that of poly(ADP-ribose) polymerase. Identification of two functionally distinct DNA binding regions within DNA ligase III. J. Biol. Chem., 274, 21679-21687.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21679-21687
    • Mackey, Z.B.1    Niedergang, C.2    Murcia, J.M.3    Leppard, J.4    Au, K.5    Chen, J.6    De Murcia, G.7    Tomkinson, A.E.8
  • 44
    • 0032964122 scopus 로고    scopus 로고
    • DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B
    • Meinke, G. and Sigler, P.B. (1999) DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B. Nature Struct. Biol., 6, 471-477.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 471-477
    • Meinke, G.1    Sigler, P.B.2
  • 45
    • 0030815133 scopus 로고    scopus 로고
    • RASTER3D: Photorealistic molecular graphics
    • Merritt, E.A. and Bacon, D.J. (1997) RASTER3D: photorealistic molecular graphics. Methods Enzymol., 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 46
    • 0030891201 scopus 로고    scopus 로고
    • DNA polymerase β in abasic site repair: A structurally conserved helix-hairpin-helix motif in lesion detection by base excision repair enzymes
    • Mullen, G.P. and Wilson, S.H. (1997) DNA polymerase β in abasic site repair: a structurally conserved helix-hairpin-helix motif in lesion detection by base excision repair enzymes. Biochemistry, 36, 4713-4717.
    • (1997) Biochemistry , vol.36 , pp. 4713-4717
    • Mullen, G.P.1    Wilson, S.H.2
  • 47
    • 0027479161 scopus 로고
    • OB (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin, A.G. (1993) OB (oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J., 12, 861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 48
    • 0030941295 scopus 로고    scopus 로고
    • XRCC1 protein interacts with one of two distinct forms of DNA ligase III
    • Nash, R.A., Caldecott, K.W., Barnes, D.E. and Lindahl, T. (1997) XRCC1 protein interacts with one of two distinct forms of DNA ligase III. Biochemistry, 36, 5207-5211.
    • (1997) Biochemistry , vol.36 , pp. 5207-5211
    • Nash, R.A.1    Caldecott, K.W.2    Barnes, D.E.3    Lindahl, T.4
  • 49
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 50
    • 0033553405 scopus 로고    scopus 로고
    • Footprinting of chlorella virus DNA ligase bound at a nick in duplex DNA
    • Odell, M. and Shuman, S. (1999) Footprinting of Chlorella virus DNA ligase bound at a nick in duplex DNA. J. Biol. Chem., 274, 14032-14039.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14032-14039
    • Odell, M.1    Shuman, S.2
  • 51
    • 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. Methods Enzymol., 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 52
    • 0032530708 scopus 로고    scopus 로고
    • Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 Å resolution
    • Peat, T.S., Newman, J., Waldo, G.S., Berendzen, J. and Terwilliger, T.C. (1998) Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 Å resolution. Structure, 6, 1207-1214.
    • (1998) Structure , vol.6 , pp. 1207-1214
    • Peat, T.S.1    Newman, J.2    Waldo, G.S.3    Berendzen, J.4    Terwilliger, T.C.5
  • 53
    • 0031009811 scopus 로고    scopus 로고
    • Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength X-ray diffraction on the selenomethioninyl protein at 2.9-Å resolution
    • Raghunathan, S., Ricard, C.S., Lohman, T.M. and Waksman, G. (1997) Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength X-ray diffraction on the selenomethioninyl protein at 2.9-Å resolution. Proc. Natl Acad. Sci. USA, 94, 6652-6657.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6652-6657
    • Raghunathan, S.1    Ricard, C.S.2    Lohman, T.M.3    Waksman, G.4
  • 55
    • 0032032172 scopus 로고    scopus 로고
    • Surface-exposed phenylalanines in the RNP1/ RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis
    • Schindler, T., Perl, D., Graumann, P., Sieber, V., Marahiel, M.A. and Schmid, F.X. (1998) Surface-exposed phenylalanines in the RNP1/ RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. Proteins, 30, 401-406.
    • (1998) Proteins , vol.30 , pp. 401-406
    • Schindler, T.1    Perl, D.2    Graumann, P.3    Sieber, V.4    Marahiel, M.A.5    Schmid, F.X.6
  • 57
    • 0031002350 scopus 로고    scopus 로고
    • The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif
    • Sette, M., van Tilborg, P., Spurio, R., Kaptein, R., Paci, M., Gualerzi, C.O. and Boelens, R. (1997) The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif. EMBO J., 16, 1436-1443.
    • (1997) EMBO J. , vol.16 , pp. 1436-1443
    • Sette, M.1    Van Tilborg, P.2    Spurio, R.3    Kaptein, R.4    Paci, M.5    Gualerzi, C.O.6    Boelens, R.7
  • 58
    • 0029056990 scopus 로고
    • RNA capping enzyme and DNA ligase: A superfamily of covalent nucleotidyl transferases
    • Shuman, S. and Schwer, B. (1995) RNA capping enzyme and DNA ligase: a superfamily of covalent nucleotidyl transferases. Mol. Microbiol., 17, 405-410.
    • (1995) Mol. Microbiol. , vol.17 , pp. 405-410
    • Shuman, S.1    Schwer, B.2
  • 60
    • 0028606031 scopus 로고
    • A unified polymerase mechanism for nonhomologous DNA and RNA polymerases
    • Steitz, T.A., Smerdon, S.J., Jäger, J. and Joyce, C.M. (1994) A unified polymerase mechanism for nonhomologous DNA and RNA polymerases. Science, 266, 2022-2025.
    • (1994) Science , vol.266 , pp. 2022-2025
    • Steitz, T.A.1    Smerdon, S.J.2    Jäger, J.3    Joyce, C.M.4
  • 61
    • 0029938467 scopus 로고    scopus 로고
    • Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7
    • Subramanya, H.S., Doherty, A.J., Ashford, S.R. and Wigley, D.B. (1996) Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. Cell, 85, 607-615.
    • (1996) Cell , vol.85 , pp. 607-615
    • Subramanya, H.S.1    Doherty, A.J.2    Ashford, S.R.3    Wigley, D.B.4
  • 63
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger, T.C. and Berendzen, J. (1999) Automated MAD and MIR structure solution. Acta Crystallogr. D, 55, 849-861.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 64
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer, M.M., Ahern, H., Xing, D., Cunningham, R.P. and Tainer, J.A. (1995) Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J., 14, 4108-4120.
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 66
    • 0031260117 scopus 로고    scopus 로고
    • Mammalian DNA ligases
    • Tomkinson, A.E. and Levin, D.S. (1997) Mammalian DNA ligases. BioEssays, 19, 893-901.
    • (1997) BioEssays , vol.19 , pp. 893-901
    • Tomkinson, A.E.1    Levin, D.S.2
  • 67
    • 0031972353 scopus 로고    scopus 로고
    • Structure and function of mammalian DNA ligases
    • Tomkinson, A.E. and Mackey, Z.B. (1998) Structure and function of mammalian DNA ligases. Mutat. Res., 407, 1-9.
    • (1998) Mutat. Res. , vol.407 , pp. 1-9
    • Tomkinson, A.E.1    Mackey, Z.B.2
  • 68
    • 0033080784 scopus 로고    scopus 로고
    • Biochemical properties of a high fidelity DNA ligase from Thermus species AK16D
    • Tong, J., Cao, W. and Barany, F. (1999) Biochemical properties of a high fidelity DNA ligase from Thermus species AK16D. Nucleic Acids Res., 27, 788-794.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 788-794
    • Tong, J.1    Cao, W.2    Barany, F.3
  • 69
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar, S.S., Soultanas, P., Dillingham, M.S., Subramanya, H.S. and Wigley, D.B. (1999) Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell, 97, 75-84.
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 70
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A.C., Laskwoski, R.A. and Thornton, J.M. (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng., 8, 127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskwoski, R.A.2    Thornton, J.M.3
  • 71
    • 0029024927 scopus 로고
    • Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination
    • Wei, Y.F. et al. (1995) Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination. Mol. Cell. Biol, 15, 3206-3216.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 3206-3216
    • Wei, Y.F.1
  • 72
    • 0026781934 scopus 로고
    • Analysis of the formation of AMP-DNA intermediate and the successive reaction by human DNA ligases I and II
    • Yang, S.-W. and Chan, Y.H. (1992) Analysis of the formation of AMP-DNA intermediate and the successive reaction by human DNA ligases I and II. J. Biol. Chem., 267, 8117-8122.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8117-8122
    • Yang, S.-W.1    Chan, Y.H.2
  • 73
    • 0032476599 scopus 로고    scopus 로고
    • Structure of an XRCC1 BRCT domain: A new protein-protein interaction module
    • Zhang, X. et al. (1998) Structure of an XRCC1 BRCT domain: a new protein-protein interaction module. EMBO J., 17, 6404-6411.
    • (1998) EMBO J. , vol.17 , pp. 6404-6411
    • Zhang, X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.