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Volumn 13, Issue 11, 2005, Pages 1665-1675

Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1″-phosphate dephosphorylation by a conserved domain of nsP3

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; NONSTRUCTURAL PROTEIN 3; PHOSPHATASE; PROTEIN; UNCLASSIFIED DRUG;

EID: 27644505258     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.07.022     Document Type: Article
Times cited : (159)

References (66)
  • 1
    • 0038047136 scopus 로고    scopus 로고
    • The crystal structure of AF1521, a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A
    • M.D. Allen, A.M. Buckle, S.C. Cordell, J. Lowe, and M. Bycroft The crystal structure of AF1521, a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A J. Mol. Biol. 330 2003 503 511
    • (2003) J. Mol. Biol. , vol.330 , pp. 503-511
    • Allen, M.D.1    Buckle, A.M.2    Cordell, S.C.3    Lowe, J.4    Bycroft, M.5
  • 3
    • 0000030013 scopus 로고
    • Mayaro virus: A new human disease agent. II. Isolation from blood of patients in Trinidad
    • C.R. Anderson, W.G. Downs, G.H. Wattley, N.W. Ahin, and A.A. Reese Mayaro virus: a new human disease agent. II. Isolation from blood of patients in Trinidad Am. J. Trop. Med. Hyg. 6 1954 1012 1016
    • (1954) Am. J. Trop. Med. Hyg. , vol.6 , pp. 1012-1016
    • Anderson, C.R.1    Downs, W.G.2    Wattley, G.H.3    Ahin, N.W.4    Reese, A.A.5
  • 4
    • 0028958236 scopus 로고
    • Effect of methyltransferase inhibitors on the regulation of baculovirus protein synthesis
    • C. Bach, A. Cramer, and C. Scholtissek Effect of methyltransferase inhibitors on the regulation of baculovirus protein synthesis J. Gen, Virol. 76 1995 1025 1032
    • (1995) J. Gen, Virol. , vol.76 , pp. 1025-1032
    • Bach, C.1    Cramer, A.2    Scholtissek, C.3
  • 6
    • 7644238616 scopus 로고    scopus 로고
    • The severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor
    • K. Bhardwaj, L. Guarino, and C.C. Kao The severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor J. Virol. 78 2004 12218 12224
    • (2004) J. Virol. , vol.78 , pp. 12218-12224
    • Bhardwaj, K.1    Guarino, L.2    Kao, C.C.3
  • 8
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for Protein Crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 Suite: programs for Protein Crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 9
    • 0029146877 scopus 로고
    • CarP, involved in pyrimidine regulation of the Escherichia coli carbamoyl-phosphate synthetase operon encodes a sequence-specific DNA-binding protein identical to XerB and PepA, also required for resolution of ColEI multimers
    • D. Charlier, G. Hassanzadeh, A. Kholti, D. Gigot, A. Pierard, and N. Glansdorff CarP, involved in pyrimidine regulation of the Escherichia coli carbamoyl-phosphate synthetase operon encodes a sequence-specific DNA-binding protein identical to XerB and PepA, also required for resolution of ColEI multimers J. Mol. Biol. 250 1995 392 406
    • (1995) J. Mol. Biol. , vol.250 , pp. 392-406
    • Charlier, D.1    Hassanzadeh, G.2    Kholti, A.3    Gigot, D.4    Pierard, A.5    Glansdorff, N.6
  • 12
    • 0027937762 scopus 로고
    • TRNA splicing in yeast and wheat germ. a cyclic phosphodiesterase implicated in the metabolism of ADP-ribose 1″-2″ cyclic phosphate
    • G.M. Culver, S.A. Consaul, K.T. Tycowski, W. Filipowicz, and E.M. Phizicky tRNA splicing in yeast and wheat germ. A cyclic phosphodiesterase implicated in the metabolism of ADP-ribose 1″-2″ cyclic phosphate J. Biol. Chem. 269 1994 24928 24934
    • (1994) J. Biol. Chem. , vol.269 , pp. 24928-24934
    • Culver, G.M.1    Consaul, S.A.2    Tycowski, K.T.3    Filipowicz, W.4    Phizicky, E.M.5
  • 13
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D. D'Amours, S. Desnoyers, I. D'Silva, and G.G. Poirier Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions Biochem. J. 342 1999 249 268
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 17
    • 0028175752 scopus 로고
    • Cyclophilin residues that affect the noncompetitive inhibition of the protein serine phosphatase activity of Calcineurin by the cyclophilin- cyclophorin a complex
    • F.A. Etzkorn, Z.Y. Chang, L.A. Stoltz, and C.T. Walsh Cyclophilin residues that affect the noncompetitive inhibition of the protein serine phosphatase activity of Calcineurin by the cyclophilin-cyclophorin A complex Biochemistry 33 1994 2380 2388
    • (1994) Biochemistry , vol.33 , pp. 2380-2388
    • Etzkorn, F.A.1    Chang, Z.Y.2    Stoltz, L.A.3    Walsh, C.T.4
  • 18
    • 21444447037 scopus 로고    scopus 로고
    • Functional characterisation of XendoU, the endoribonuclease involved in small nucleolar RNA biosynthesis
    • U. Gioia, P. Laneve, M. Dlakic, M. Arceci, I. Bozzoni, and E. Caffarelli Functional characterisation of XendoU, the endoribonuclease involved in small nucleolar RNA biosynthesis J. Biol. Chem. 280 2005 18996 19002
    • (2005) J. Biol. Chem. , vol.280 , pp. 18996-19002
    • Gioia, U.1    Laneve, P.2    Dlakic, M.3    Arceci, M.4    Bozzoni, I.5    Caffarelli, E.6
  • 19
    • 0242720705 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome: Global initiatives for disease diagnosis
    • D.A. Groneberg, L. Zhang, T. Welte, P. Zabel, and K.F. Chung Severe acute respiratory syndrome: global initiatives for disease diagnosis QJM 96 2003 845 852
    • (2003) QJM , vol.96 , pp. 845-852
    • Groneberg, D.A.1    Zhang, L.2    Welte, T.3    Zabel, P.4    Chung, K.F.5
  • 20
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • L. Holm, and C. Sander Protein structure comparison by alignment of distance matrices J. Mol. Biol. 233 1993 123 138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 23
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 1991 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
  • 25
    • 11144348687 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme 2: A functional receptor for SARS coronavirus
    • J.H. Kuhn, W. Li, H. Choe, and M. Farzan Angiotensin-converting enzyme 2: a functional receptor for SARS coronavirus Cell. Mol. Life Sci. 61 2004 2738 2743
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 2738-2743
    • Kuhn, J.H.1    Li, W.2    Choe, H.3    Farzan, M.4
  • 26
    • 14144253106 scopus 로고    scopus 로고
    • Structure and mechanism of ADP-ribose-1″-monophosphatase (Appr-1″-pase), a ubiquitous cellular processing enzyme
    • D. Kumaran, S. Eswaramoorthy, F.W. Studier, and S. Swaminathan Structure and mechanism of ADP-ribose-1″-monophosphatase (Appr-1″-pase), a ubiquitous cellular processing enzyme Protein Sci. 14 2005 719 726
    • (2005) Protein Sci. , vol.14 , pp. 719-726
    • Kumaran, D.1    Eswaramoorthy, S.2    Studier, F.W.3    Swaminathan, S.4
  • 27
    • 0003208239 scopus 로고    scopus 로고
    • Coronaviruses
    • D.M. Knipe P.M. Howley Lippincott Philadelphia, PA
    • M.M.C. Lai, and K.V. Holmes Coronaviruses D.M. Knipe P.M. Howley Fields Virology 2001 Lippincott Philadelphia, PA 1163 1185
    • (2001) Fields Virology , pp. 1163-1185
    • Lai, M.M.C.1    Holmes, K.V.2
  • 28
    • 0030852350 scopus 로고    scopus 로고
    • Automated refinement for protein crystallography
    • C. Carter B. Sweet Academic Press Orlando, FL
    • V.S. Lamzin, and K.S. Wilson Automated refinement for protein crystallography C. Carter B. Sweet Methods in Enzymology 1997 Academic Press Orlando, FL 269 305
    • (1997) Methods in Enzymology , pp. 269-305
    • Lamzin, V.S.1    Wilson, K.S.2
  • 35
    • 0025157279 scopus 로고
    • A highly specific phosphatase from Saccharomyces cerevisiae implicated in tRNA splicing
    • S.M. McCraith, and E.M. Phizicky A highly specific phosphatase from Saccharomyces cerevisiae implicated in tRNA splicing Mol. Cell. Biol. 10 1990 1049 1055
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1049-1055
    • McCraith, S.M.1    Phizicky, E.M.2
  • 36
    • 0028237249 scopus 로고
    • Peptidase activity of Escherichia coli aminopeptidase a is not required for its role in Xer site-specific recombination
    • R. McCulloch, M.E. Burke, and D.J. Sherratt Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination Mol. Microbiol. 12 1994 241 251
    • (1994) Mol. Microbiol. , vol.12 , pp. 241-251
    • McCulloch, R.1    Burke, M.E.2    Sherratt, D.J.3
  • 40
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • A.G. Murzin, S.E. Brenner, T. Hubbard, and C. Chothia SCOP: a structural classification of proteins database for the investigation of sequences and structures J. Mol. Biol. 247 1995 536 540
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor 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
  • 42
    • 0037126614 scopus 로고    scopus 로고
    • Sequence requirements for RNA strand transfer during nidovirus discontinuous subgenomic RNA synthesis
    • A.O. Pasternak, E. van den Born, W.J. Spaan, and E.J. Snijder Sequence requirements for RNA strand transfer during nidovirus discontinuous subgenomic RNA synthesis EMBO J. 20 2001 7220 7228
    • (2001) EMBO J. , vol.20 , pp. 7220-7228
    • Pasternak, A.O.1    Van Den Born, E.2    Spaan, W.J.3    Snijder, E.J.4
  • 43
    • 0020710638 scopus 로고
    • Precise excision of intervening sequences from precursor tRNAs by a membrane-associated yeast endonuclease
    • C.L. Peebles, P. Gegenheimer, and J. Abelson Precise excision of intervening sequences from precursor tRNAs by a membrane-associated yeast endonuclease Cell 32 1983 525 536
    • (1983) Cell , vol.32 , pp. 525-536
    • Peebles, C.L.1    Gegenheimer, P.2    Abelson, J.3
  • 44
    • 0026737922 scopus 로고
    • MacroH2A, a core histone containing a large nonhistone region
    • J.R. Pehrson, and V.A. Fried MacroH2A, a core histone containing a large nonhistone region Science 257 1992 1398 1400
    • (1992) Science , vol.257 , pp. 1398-1400
    • Pehrson, J.R.1    Fried, V.A.2
  • 45
    • 0032526621 scopus 로고    scopus 로고
    • Evolutionary conservation of histone macroH2A subtypes and domains
    • J.R. Pehrson, and R.N. Fuji Evolutionary conservation of histone macroH2A subtypes and domains Nucleic Acids Res. 26 1998 2837 2842
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2837-2842
    • Pehrson, J.R.1    Fuji, R.N.2
  • 47
    • 0027392502 scopus 로고
    • Pre-tRNA splicing: Variation on a theme or exception to the rule?
    • E.M. Phizicky, and C.L. Greer Pre-tRNA splicing: variation on a theme or exception to the rule? Trends Biochem. Sci. 18 1993 31 34
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 31-34
    • Phizicky, E.M.1    Greer, C.L.2
  • 48
    • 0033997036 scopus 로고    scopus 로고
    • Comparison of sequence profiles. Strategies for structural predictions using sequence information
    • L. Rychlewski, L. Jaroszewski, W. Li, and A. Godzik Comparison of sequence profiles. Strategies for structural predictions using sequence information Protein Sci. 9 2000 232 241
    • (2000) Protein Sci. , vol.9 , pp. 232-241
    • Rychlewski, L.1    Jaroszewski, L.2    Li, W.3    Godzik, A.4
  • 50
    • 0034009771 scopus 로고    scopus 로고
    • Genome structure of Sagiyama virus and its relatedness to other alphaviruses
    • Y. Shirako, and Y. Yamaguchi Genome structure of Sagiyama virus and its relatedness to other alphaviruses J. Gen. Virol. 81 2000 1353 1360
    • (2000) J. Gen. Virol. , vol.81 , pp. 1353-1360
    • Shirako, Y.1    Yamaguchi, Y.2
  • 51
    • 13844312497 scopus 로고    scopus 로고
    • A highly specific phosphatase that acts on ADP-ribose 1″-phosphate, a metabolite of tRNA splicing in Saccharomyces cerevisiae
    • N.P. Shull, S.L. Spinelli, and E.M. Phizicky A highly specific phosphatase that acts on ADP-ribose 1″-phosphate, a metabolite of tRNA splicing in Saccharomyces cerevisiae Nucleic Acids Res. 33 2005 650 660
    • (2005) Nucleic Acids Res. , vol.33 , pp. 650-660
    • Shull, N.P.1    Spinelli, S.L.2    Phizicky, E.M.3
  • 53
    • 0028889561 scopus 로고
    • Two-metal ion mechanism of bovine lens leucine aminopeptidase: Active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography
    • N. Sträter, and W.N. Lipscomb Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography Biochemistry 34 1995 14792 14800
    • (1995) Biochemistry , vol.34 , pp. 14792-14800
    • Sträter, N.1    Lipscomb, W.N.2
  • 54
    • 0344931801 scopus 로고    scopus 로고
    • X-ray structure of aminopeptidase a from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination
    • N. Sträter, D.J. Sherratt, and S.D. Colloms X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination EMBO J. 18 1999 4513 4522
    • (1999) EMBO J. , vol.18 , pp. 4513-4522
    • Sträter, N.1    Sherratt, D.J.2    Colloms, S.D.3
  • 55
    • 0021319456 scopus 로고
    • Complete nucleotide sequence of the genomic RNA of Sindbis virus
    • E.G. Strauss, C.M. Rice, and J.H. Strauss Complete nucleotide sequence of the genomic RNA of Sindbis virus Virology 133 1984 92 110
    • (1984) Virology , vol.133 , pp. 92-110
    • Strauss, E.G.1    Rice, C.M.2    Strauss, J.H.3
  • 56
    • 0141993465 scopus 로고    scopus 로고
    • Statistical density modification using local pattern matching
    • T.C. Terwilliger Statistical density modification using local pattern matching Acta Crystallogr. D59 2003 1688 1701
    • (2003) Acta Crystallogr. , vol.59 , pp. 1688-1701
    • Terwilliger, T.C.1
  • 60
    • 0036827714 scopus 로고    scopus 로고
    • Role of the alfalfa mosaic virus methyltransferase-like domain in negative-strand RNA synthesis
    • A.C. Vlot, A. Menard, and J.F. Bol Role of the alfalfa mosaic virus methyltransferase-like domain in negative-strand RNA synthesis J. Virol. 76 2002 11321 11328
    • (2002) J. Virol. , vol.76 , pp. 11321-11328
    • Vlot, A.C.1    Menard, A.2    Bol, J.F.3
  • 61
    • 0038681984 scopus 로고    scopus 로고
    • MRNA cap-1 methyltransferase in the SARS genome
    • M. von Grotthuss, L.S. Wyrwicz, and L. Rychlewski mRNA cap-1 methyltransferase in the SARS genome Cell 113 2003 701 702
    • (2003) Cell , vol.113 , pp. 701-702
    • Von Grotthuss, M.1    Wyrwicz, L.S.2    Rychlewski, L.3
  • 62
    • 0001607723 scopus 로고
    • Distantly related sequences in the α-subunits and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • J.E. Walker, M. Saraste, M.J. Runswick, and N.J. Gay Distantly related sequences in the α-subunits and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold EMBO J. 1 1982 945 951
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 63
    • 0029142527 scopus 로고
    • A continuous spectrophotometric assay for phosphorylase kinase
    • Z.-X. Wang, Q. Cheng, and S.D. Killilea A continuous spectrophotometric assay for phosphorylase kinase Anal. Biochem. 230 1995 55 61
    • (1995) Anal. Biochem. , vol.230 , pp. 55-61
    • Wang, Z.-X.1    Cheng, Q.2    Killilea, S.D.3
  • 64
    • 0026684153 scopus 로고
    • A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems
    • M.R. Webb A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems Proc. Natl. Acad. Sci. USA 89 1992 4884 4887
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4884-4887
    • Webb, M.R.1
  • 65
  • 66
    • 0035980126 scopus 로고    scopus 로고
    • The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond
    • J. Ziebuhr, V. Thiel, and A.E. Gorbalenya The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond J. Biol. Chem. 276 2001 33220 33232
    • (2001) J. Biol. Chem. , vol.276 , pp. 33220-33232
    • Ziebuhr, J.1    Thiel, V.2    Gorbalenya, A.E.3


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