메뉴 건너뛰기




Volumn 7, Issue , 2007, Pages

Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; URACIL DNA GLYCOSIDASE; VIRUS PROTEIN;

EID: 34547629029     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-7-45     Document Type: Article
Times cited : (43)

References (40)
  • 2
    • 33645639121 scopus 로고    scopus 로고
    • Vaccinia virus uracil DNA glycosylase interacts with the A20 protein to form a heterodimeric processivity factor for the viral DNA polymerase
    • 10.1074/jbc.M511239200. 16326701
    • Vaccinia virus uracil DNA glycosylase interacts with the A20 protein to form a heterodimeric processivity factor for the viral DNA polymerase. ES Stanitsa L Arps P Traktman, J Biol Chem 2006 281 3439 3451 10.1074/jbc. M511239200 16326701
    • (2006) J Biol Chem , vol.281 , pp. 3439-3451
    • Stanitsa, E.S.1    Arps, L.2    Traktman, P.3
  • 3
    • 0029845801 scopus 로고    scopus 로고
    • Mutations in active-site residues of the uracil-DNA glycosylase encoded by vaccinia virus are incompatible with virus viability
    • 8892920
    • Mutations in active-site residues of the uracil-DNA glycosylase encoded by vaccinia virus are incompatible with virus viability. KS Ellison W Peng G McFadden, J Virology 1996 70 7965 7973 8892920
    • (1996) J Virology , vol.70 , pp. 7965-7973
    • Ellison, K.S.1    Peng, W.2    McFadden, G.3
  • 4
    • 0037213268 scopus 로고    scopus 로고
    • Vaccinia virus uracil DNA glycosylase has an essential role in DNA synthesis that is independent of its glycosylase activity: Catalytic site mutations reduce virulence but not virus replication in cultured cells
    • 12477821. 10.1128/JVI.77.1.159-166.2003
    • Vaccinia virus uracil DNA glycosylase has an essential role in DNA synthesis that is independent of its glycosylase activity: catalytic site mutations reduce virulence but not virus replication in cultured cells. FS De Silva B Moss, J Virology 2003 77 159 166 12477821 10.1128/JVI.77.1.159-166.2003
    • (2003) J Virology , vol.77 , pp. 159-166
    • De Silva, F.S.1    Moss, B.2
  • 5
    • 0036943963 scopus 로고    scopus 로고
    • Mapping interaction sites of the A20R protein component of the vaccinia virus DNA replication complex
    • 10.1006/viro.2002.1721. 12490386
    • Mapping interaction sites of the A20R protein component of the vaccinia virus DNA replication complex. K Ishii B Moss, Virology 2002 303 232 239 10.1006/viro.2002.1721 12490386
    • (2002) Virology , vol.303 , pp. 232-239
    • Ishii, K.1    Moss, B.2
  • 6
    • 9444293216 scopus 로고    scopus 로고
    • SCOP database. http://scop.mrc-lmb.cam.ac.uk/scop
    • SCOP Database
  • 7
    • 34547642414 scopus 로고    scopus 로고
    • ProFace server. http://www.boseinst.ernet.in/resources/bioinfo/stag.html/
    • ProFace Server
  • 8
    • 33746276951 scopus 로고    scopus 로고
    • ProFace: A server for the analysis of the physicochemical features of protein-protein interfaces
    • 16759379. 10.1186/1472-6807-6-11
    • ProFace: a server for the analysis of the physicochemical features of protein-protein interfaces. RP Saha RP Bahadur A Pal S Mandal P Chakrabarti, BMC Struct Biol 2006 6 11 16 16759379 10.1186/1472-6807-6-11
    • (2006) BMC Struct Biol , vol.6 , pp. 11-16
    • Saha, R.P.1    Bahadur, R.P.2    Pal, A.3    Mandal, S.4    Chakrabarti, P.5
  • 9
    • 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
    • 10.1002/(SICI)1097-0134(19990401)35:1<13::AID-PROT2>3.0.CO;2-2. 10090282
    • Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: Structure and glycosylase mechanism revisited. G Xiao M Tordova J Jagadeesh AC Drohat JT Stivers GL Gilliland, Proteins 1999 35 13 24 10.1002/(SICI)1097-0134(19990401)35:1<13::AID- PROT2>3.0.CO;2-2 10090282
    • (1999) Proteins , vol.35 , pp. 13-24
    • Xiao, G.1    Tordova, M.2    Jagadeesh, J.3    Drohat, A.C.4    Stivers, J.T.5    Gilliland, G.L.6
  • 10
    • 0033554424 scopus 로고    scopus 로고
    • Role of electrophilic and general base catalysis in the mechanism of Escherichia coli uracil DNA glycosylase
    • 10.1021/bi9910878. 10508389
    • Role of electrophilic and general base catalysis in the mechanism of Escherichia coli uracil DNA glycosylase. AC Drohat J Jagadeesh E Ferguson JT Stivers, Biochemistry 1999 38 11866 11875 10.1021/bi9910878 10508389
    • (1999) Biochemistry , vol.38 , pp. 11866-11875
    • Drohat, A.C.1    Jagadeesh, J.2    Ferguson, E.3    Stivers, J.T.4
  • 11
    • 0033579953 scopus 로고    scopus 로고
    • Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase
    • 10.1021/bi9818669. 9893991
    • Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase. JT Stivers KW Pankiewicz KA Watanabe, Biochemistry 1999 38 952 963 10.1021/bi9818669 9893991
    • (1999) Biochemistry , vol.38 , pp. 952-963
    • Stivers, J.T.1    Pankiewicz, K.W.2    Watanabe, K.A.3
  • 12
    • 0035954406 scopus 로고    scopus 로고
    • Reconstructing the substrate for uracil DNA glycosylase: Tracking the transmission of binding energy in catalysis
    • 10.1021/bi010622c. 11412125
    • Reconstructing the substrate for uracil DNA glycosylase: tracking the transmission of binding energy in catalysis. YL Jiang JT Stivers, Biochemistry 2001 40 7710 7719 10.1021/bi010622c 11412125
    • (2001) Biochemistry , vol.40 , pp. 7710-7719
    • Jiang, Y.L.1    Stivers, J.T.2
  • 13
    • 0032167424 scopus 로고    scopus 로고
    • Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA
    • 9724657. 10.1093/emboj/17.17.5214
    • Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. SS Parikh CD Mol G Slupphaug S Bharati HE Krokan JA Tainer, EMBO J 1998 17 5214 5226 9724657 10.1093/emboj/17.17.5214
    • (1998) EMBO J , vol.17 , pp. 5214-5226
    • Parikh, S.S.1    Mol, C.D.2    Slupphaug, G.3    Bharati, S.4    Krokan, H.E.5    Tainer, J.A.6
  • 14
    • 0032822325 scopus 로고    scopus 로고
    • Envisioning the molecular choreography of DNA base excision repair
    • 10.1016/S0959-440X(99)80006-2. 10047578
    • Envisioning the molecular choreography of DNA base excision repair. SS Parikh CD Mol DJ Hosfield JA Tainer, Curr Opin Struct Biol 1999 9 37 47 10.1016/S0959-440X(99)80006-2 10047578
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 37-47
    • Parikh, S.S.1    Mol, C.D.2    Hosfield, D.J.3    Tainer, J.A.4
  • 15
    • 0034625082 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase-DNA substrate and product structures: Conformational strain promotes catalytic efficiency by coupled stereoelectronic effects
    • 10805771. 10.1073/pnas.97.10.5083
    • Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects. SS Parikh G Walcher GD Jones G Slupphaug HE Krokan GM Blackburn JA Tainer, Proc Natl Acad Sci USA 2000 97 5083 5088 10805771 10.1073/pnas.97.10. 5083
    • (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
  • 17
    • 0035907352 scopus 로고    scopus 로고
    • The role of leucine 191 of Escherichia coli uracil DNA glycosylase in the formation of a highly stable complex with the substrate mimic, Ugi, and in uracil excision from the synthetic substrates
    • 10.1074/jbc.M011166200
    • The role of leucine 191 of Escherichia coli uracil DNA glycosylase in the formation of a highly stable complex with the substrate mimic, Ugi, and in uracil excision from the synthetic substrates. P Handa S Roy U Varshney, J Biol Chem 2001 20 17324 17331 10.1074/jbc.M011166200
    • (2001) J Biol Chem , vol.20 , pp. 17324-17331
    • Handa, P.1    Roy, S.2    Varshney, U.3
  • 18
    • 0033605817 scopus 로고    scopus 로고
    • Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase
    • 10.1006/jmbi.1999.2605. 10080896
    • Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase. CD Putnam MJN Shroyer AJ Lundquist CD Mol AS Arvai DW Mosbaugh JA Tainer, J Mol Biol 1999 287 331 346 10.1006/jmbi.1999.2605 10080896
    • (1999) J Mol Biol , vol.287 , pp. 331-346
    • Putnam, C.D.1    Shroyer, M.J.N.2    Lundquist, A.J.3    Mol, C.D.4    Arvai, A.S.5    Mosbaugh, D.W.6    Tainer, J.A.7
  • 19
    • 3643055084 scopus 로고    scopus 로고
    • X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. the structure elucidation of a prokaryotic UDG
    • 9776748. 10.1093/nar/26.21.4880
    • X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG. R Ravishankar M Bidya Sagar S Roy K Purnapatre P Handa U Varshney M Vijayan, Nucleic Acids Research 1998 26 4880 4887 9776748 10.1093/nar/26.21.4880
    • (1998) Nucleic Acids Research , vol.26 , pp. 4880-4887
    • Ravishankar, R.1    Bidya Sagar, M.2    Roy, S.3    Purnapatre, K.4    Handa, P.5    Varshney, U.6    Vijayan, M.7
  • 20
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracil-DNA glycosylase
    • 10.1038/373487a0. 7845459
    • The structural basis of specific base-excision repair by uracil-DNA glycosylase. R Savva K McAuley-Hecht T Brown L Pearl, Nature 1995 373 487 493 10.1038/373487a0 7845459
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R.1    McAuley-Hecht, K.2    Brown, T.3    Pearl, L.4
  • 21
    • 0034734380 scopus 로고    scopus 로고
    • Lessons learned from structural results on uracil-DNA glycosylase
    • 10.1016/S0921-8777(00)00026-4. 10946228
    • Lessons learned from structural results on uracil-DNA glycosylase. SS Parikh CD Putnam JA Tainer, Mutation Research 2000 460 183 199 10.1016/S0921-8777(00)00026-4 10946228
    • (2000) Mutation Research , vol.460 , pp. 183-199
    • Parikh, S.S.1    Putnam, C.D.2    Tainer, J.A.3
  • 22
    • 0003115798 scopus 로고    scopus 로고
    • A WWW service system for automatic comparison of protein structures
    • A WWW service system for automatic comparison of protein structures. G Lu, Protein Data Bank Quarterly Newsletter 1996 78 10 11
    • (1996) Protein Data Bank Quarterly Newsletter , vol.78 , pp. 10-11
    • Lu, G.1
  • 23
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis
    • 10.1016/0092-8674(95)90290-2. 7697717
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. CD Mol AS Arvai G Slupphaug B Kavil I Alseth HE Krokan JA Tainer, Cell 1995 80 869 878 10.1016/0092-8674(95)90290-2 7697717
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavil, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 24
    • 0038455931 scopus 로고    scopus 로고
    • Flexibility revealed by the 1.85 Å crystal structure of the beta sliding-clamp subunit of Escherichia coli DNA polymerase III
    • 10.1107/S0907444903009958. 12832762
    • Flexibility revealed by the 1.85 Å crystal structure of the beta sliding-clamp subunit of Escherichia coli DNA polymerase III. AJ Oakley P Prosselkov G Wijffels JL Beck MCJ Wilce NE Dixon, Acta Crystallogr D Biol Crystallogr 2003 59 Pt 7 1192 1199 10.1107/S0907444903009958 12832762
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , Issue.PART 7 , pp. 1192-1199
    • Oakley, A.J.1    Prosselkov, P.2    Wijffels, G.3    Beck, J.L.4    Wilce, M.C.J.5    Dixon, N.E.6
  • 26
    • 0032692565 scopus 로고    scopus 로고
    • Building a replisome from interacting pieces: Sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex
    • 10.1016/S0092-8674(00)81647-5. 10535734
    • Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex. Y Shamoo TA Steitz, Cell 1999 99 155 166 10.1016/S0092-8674(00)81647-5 10535734
    • (1999) Cell , vol.99 , pp. 155-166
    • Shamoo, Y.1    Steitz, T.A.2
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Processing of X-ray diffraction data collected in oscillation mode. Z Otwinowski W Minor, Methods Enzymol 1997 276 307 326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • 10.1107/S090744499900935X. 10531521
    • The finer things in X-ray diffraction data collection. JW Pflugrath, Acta Crystallogr D Biol Crystallogr 1999 55 Pt 10 1718 1725 10.1107/ S090744499900935X 10531521
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , Issue.PART 10 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 31
    • 0013054388 scopus 로고    scopus 로고
    • Macromolecular phasing with SHELXE
    • 10.1524/zkri.217.12.644.20662
    • Macromolecular phasing with SHELXE. GM Sheldrick, Zeitschr Kristallographie 2002 217 644 650 10.1524/zkri.217.12.644.20662
    • (2002) Zeitschr Kristallographie , vol.217 , pp. 644-650
    • Sheldrick, G.M.1
  • 32
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • 10.1107/S0021889897006766
    • MOLREP: an automated program for molecular replacement. A Vagin A Teplyakov, J Appl Crystallogr 1997 30 1022 1025 10.1107/S0021889897006766
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 34
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • 10.1107/S0907444904019158
    • Coot: Model-building tools for molecular graphics. P Emsley K Cowtan, Acta Crystallogr D Biol Crystallogr 2004 D60 2126 2132 10.1107/S0907444904019158
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 35
    • 0344541116 scopus 로고    scopus 로고
    • Recent developments for the efficient crystallographic refinement of macromolecular structures
    • 10.1016/S0959-440X(98)80152-8. 9818265
    • Recent developments for the efficient crystallographic refinement of macromolecular structures. AT Brunger PD Adams LM Rice, Curr Opin Struct Biol 1998 8 606 611 10.1016/S0959-440X(98)80152-8 9818265
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 606-611
    • Brunger, A.T.1    Adams, P.D.2    Rice, L.M.3
  • 36
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • 10.1107/S0907444996012255. 15299926
    • Refinement of macromolecular structures by the maximum-likelihood method. GN Murshudov AA Vagin EJ Dodson, Acta Crystallogr D Biol Crystallogr 1997 53 Pt 3 240 255 10.1107/S0907444996012255 15299926
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 37
    • 34547645889 scopus 로고    scopus 로고
    • TLSMD server. http://skuld.bmsc.washington.edu/∼tlsmd/index.html
    • TLSMD Server
  • 38
    • 0346122798 scopus 로고    scopus 로고
    • GRASP2: Visualization, surface properties, and electrostatics of macromolecular structures and sequences
    • 14696386
    • GRASP2: visualization, surface properties, and electrostatics of macromolecular structures and sequences. D Petrev B Honig, Methods Enzymol 2003 374 492 509 14696386
    • (2003) Methods Enzymol , vol.374 , pp. 492-509
    • Petrev, D.1    Honig, B.2
  • 39
    • 34547644548 scopus 로고    scopus 로고
    • PDBSUM server. http://www.ebi.ac.uk/thornton-srv/databases/pdbsum
    • PDBSUM Server
  • 40
    • 0035175679 scopus 로고    scopus 로고
    • PDBsum: Summaries and analyses of PDB structures
    • 11125097. 10.1093/nar/29.1.221
    • PDBsum: summaries and analyses of PDB structures. RA Laskowski, Nucleic Acids Res 2001 29 221 222 11125097 10.1093/nar/29.1.221
    • (2001) Nucleic Acids Res , vol.29 , pp. 221-222
    • Laskowski, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.