메뉴 건너뛰기




Volumn 288, Issue 3, 2013, Pages 2081-2091

Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: III. atomic resolution structure of the nascent form of the adenovirus proteinase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION PATHWAY; ADENOVIRUS PROTEINASE; ATOMIC RESOLUTION STRUCTURES; COFACTORS; CONFORMATIONAL CHANGE; CYSTEINE PROTEINASE; GENERAL BASE; INACTIVE ENZYMES; INFECTIOUS VIRUS; ION PAIRS; STRUCTURAL CHANGE; STRUCTURAL DIFFERENCES; VIRAL DNA;

EID: 84872735707     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.407429     Document Type: Article
Times cited : (12)

References (49)
  • 1
    • 0017237714 scopus 로고
    • Genetic analysis of adenovirus type 2 III. Temperature sensitivity of processing viral proteins
    • Weber, J. (1976) Genetic analysis of adenovirus type 2 III. Temperature sensitivity of processing viral proteins. J. Virol. 17, 462-471
    • (1976) J. Virol. , vol.17 , pp. 462-471
    • Weber, J.1
  • 2
    • 0027390796 scopus 로고
    • Viral DNA and a viral peptide can act as cofactors of adenovirus virion proteinase activity
    • DOI 10.1038/361274a0
    • Mangel, W. F., McGrath, W. J., Toledo, D. L., and Anderson, C. W. (1993) Viral DNA and a viral peptide can act as cofactors of adenovirus virion proteinase activity. Nature 361, 274-275 (Pubitemid 23034481)
    • (1993) Nature , vol.361 , Issue.6409 , pp. 274-275
    • Mangel, W.F.1    McGrath, W.J.2    Toledo, D.L.3    Anderson, C.W.4
  • 3
    • 0027509951 scopus 로고
    • The adenovirus protease is activated by a virus-coded disulphide-linked peptide
    • DOI 10.1016/0092-8674(93)90053-S
    • Webster, A., Hay, R. T., and Kemp, G. (1993) The adenovirus protease is activated by a virus-coded disulphide-linked peptide. Cell 72, 97-104 (Pubitemid 23029696)
    • (1993) Cell , vol.72 , Issue.1 , pp. 97-104
    • Webster, A.1    Hay, R.T.2    Kemp, G.3
  • 4
    • 0030591441 scopus 로고    scopus 로고
    • Different modes of inhibition of human adenovirus proteinase, probably a cysteine proteinase, by bovine pancreatic trypsin inhibitor
    • DOI 10.1016/0014-5793(96)00569-8
    • Brown, M. T., McGrath, W. J., Toledo, D. L., and Mangel, W. F. (1996) Different modes of inhibition of human adenovirus proteinase, probably a cysteine proteinase, by bovine pancreatic trypsin inhibitor. FEBS Lett. 388, 233-237 (Pubitemid 26226368)
    • (1996) FEBS Letters , vol.388 , Issue.2-3 , pp. 233-237
    • Brown, M.T.1    McGrath, W.J.2    Toledo, D.L.3    Mangel, W.F.4
  • 8
    • 0027171113 scopus 로고
    • The active adenovirus protease is the intact L3 23K protein
    • Webster, A., and Kemp, G. (1993) The active adenovirus protease is the intact L3 23K protein. J. Gen. Virol. 74, 1415-1420 (Pubitemid 23230261)
    • (1993) Journal of General Virology , vol.74 , Issue.7 , pp. 1415-1420
    • Webster, A.1    Kemp, G.2
  • 9
    • 0029914251 scopus 로고    scopus 로고
    • Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor
    • Ding, J., McGrath, W. J., Sweet, R. M., and Mangel, W. F. (1996) Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor. EMBO J. 15, 1778-1783 (Pubitemid 26119213)
    • (1996) EMBO Journal , vol.15 , Issue.8 , pp. 1778-1783
    • Ding, J.1    McGrath, W.J.2    Sweet, R.M.3    Mangel, W.F.4
  • 10
    • 0038644484 scopus 로고    scopus 로고
    • Crystallographic structure at 1.6-A resolution of the human adenovirus proteinase in a covalent complex with its 11-amino-acid peptide cofactor: Insights on a new fold
    • DOI 10.1016/S1570-9639(03)00024-4
    • McGrath, W. J., Ding, J., Didwania, A., Sweet, R. M., and Mangel, W. F. (2003) Crystallographic structure at 1.6-Ä resolution of the human adenovirus proteinase in a covalent complex with its 11-amino-acid peptide cofactor: insights on a new fold. Biochim. Biophys. Acta 1648, 1-11 (Pubitemid 38234600)
    • (2003) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1648 , Issue.1-2 , pp. 1-11
    • McGrath, W.J.1    Ding, J.2    Didwania, A.3    Sweet, R.M.4    Mangel, W.F.5
  • 11
    • 0036292317 scopus 로고    scopus 로고
    • In the virion, the 11-amino-acid peptide cofactor pVIc is covalently linked to the adenovirus proteinase
    • DOI 10.1006/viro.2002.1394
    • McGrath, W. J., Aherne, K. S., and Mangel, W. F. (2002) In the virion, the 11-amino-acid peptide cofactor pVIc is covalently linked to the adenovirus proteinase. Virology 296, 234-240 (Pubitemid 34713263)
    • (2002) Virology , vol.296 , Issue.2 , pp. 234-240
    • McGrath, W.J.1    Aherne, K.S.2    Mangel, W.F.3
  • 12
    • 0035818427 scopus 로고    scopus 로고
    • Human adenovirus proteinase: DNA binding and stimulation of proteinase activity by DNA
    • DOI 10.1021/bi0111653
    • McGrath, W. J., Baniecki, M. L., Li, C., McWhirter, S. M., Brown, M. T., Toledo, D. L., and Mangel, W. F. (2001) Human adenovirus proteinase: DNAbinding and stimulation of proteinase activity by DNA. Biochemistry 40, 13237-13245 (Pubitemid 33043538)
    • (2001) Biochemistry , vol.40 , Issue.44 , pp. 13237-13245
    • McGrath, J.W.1    Baniecki, M.L.2    Li, C.3    McWhirter, S.M.4    Brown, M.T.5    Toledo, D.L.6    Mangel, W.F.7
  • 13
    • 0030027458 scopus 로고    scopus 로고
    • Characterization of three components of human adenovirus proteinase activity in vitro
    • DOI 10.1074/jbc.271.1.536
    • Mangel, W. F., Toledo, D. L., Brown, M. T., Martin, J. H., and McGrath, W. J. (1996) Characterization of three components of human adenovirus proteinase activity in vitro. J. Biol. Chem. 271, 536-543 (Pubitemid 26026623)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.1 , pp. 536-543
    • Mangel, W.F.1    Toledo, D.L.2    Brown, M.T.3    Martin, J.H.4    McGrath, W.J.5
  • 14
    • 0002917513 scopus 로고    scopus 로고
    • Principles of virion structure, function and assembly
    • (Chiu, W., Burnett, R. M., and Garcea, R. L., eds), Oxford University Press, Oxford
    • Casjens, S. (1997) Principles of virion structure, function and assembly. In: Structural Biology of Viruses (Chiu, W., Burnett, R. M., and Garcea, R. L., eds) pp. 3-37, Oxford University Press, Oxford
    • (1997) Structural Biology of Viruses , pp. 3-37
    • Casjens, S.1
  • 15
    • 0042823481 scopus 로고    scopus 로고
    • Transport of nucleosome core particles in semidilute DNA solutions
    • Mangenot, S., Keller, S., and Rädler, J. (2003) Transport of nucleosome core particles in semidilute DNA solutions. Biophys. J. 85, 1817-1825 (Pubitemid 37052263)
    • (2003) Biophysical Journal , vol.85 , Issue.3 , pp. 1817-1825
    • Mangenot, S.1    Keller, S.2    Radler, J.3
  • 16
    • 0029145689 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of the human adenovirus serotype 2 proteinase with peptide cofactor
    • Keefe, L. J., Ginell, S. L., Westbrook, E. M., and Anderson, C. W. (1995) Crystallization and preliminary X-ray diffraction studies of the human adenovirus serotype 2 proteinase with peptide cofactor. Protein Sci. 4, 1658-1660
    • (1995) Protein Sci. , vol.4 , pp. 1658-1660
    • Keefe, L.J.1    Ginell, S.L.2    Westbrook, E.M.3    Anderson, C.W.4
  • 17
    • 0030198630 scopus 로고    scopus 로고
    • Preparation and crystallization of a complex between human adenovirus serotype 2 proteinase and its 11-amino-acid cofactor pVIc
    • DOI 10.1006/jsbi.1996.0072
    • McGrath, W. J., Ding, J., Sweet, R. M., and Mangel, W. F. (1996) Preparation and crystallization of a complex between human adenovirus serotype 2 proteinase and its 11-amino-acid cofactor pVIc. J. Struct. Biol. 117, 77-79 (Pubitemid 26285630)
    • (1996) Journal of Structural Biology , vol.117 , Issue.1 , pp. 77-79
    • McGrath, W.J.1    Ding, J.2    Sweet, R.M.3    Mangel, W.F.4
  • 18
    • 0035807868 scopus 로고    scopus 로고
    • Roles of two conserved cysteine residues in the activation of human adenovirus proteinase
    • DOI 10.1021/bi011562d
    • McGrath, W. J., Baniecki, M. L., Peters, E., Green, D. T., and Mangel, W. F. (2001) Roles of two conserved cysteine residues in the activation of human adenovirus proteinase. Biochemistry 40, 14468-14474 (Pubitemid 33111729)
    • (2001) Biochemistry , vol.40 , Issue.48 , pp. 14468-14474
    • McGrath, W.J.1    Baniecki, M.L.2    Peters, E.3    Green, D.T.4    Mangel, W.F.5
  • 19
    • 0016115206 scopus 로고
    • Mercaptide-imidazolium ion-pair: The reactive nucleophile in papain catalysis
    • Polgár, L. (1974) Mercaptide-imidazolium ion-pair: the reactive nucleophile in papain catalysis. FEBS Lett. 47, 15-18
    • (1974) FEBS Lett. , vol.47 , pp. 15-18
    • Polgár, L.1
  • 21
    • 0027548474 scopus 로고
    • Expression and purification of the adenovirus proteinase polypeptide and of a synthetic proteinase substrate
    • Anderson, C. W. (1993) Expression and purification of the adenovirus proteinase polypeptide and of a synthetic proteinase substrate. Protein Expr. Purif. 4, 8-15
    • (1993) Protein Expr. Purif. , vol.4 , pp. 8-15
    • Anderson, C.W.1
  • 22
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326 (Pubitemid 19277112)
    • (1989) Analytical Biochemistry , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0031053055 scopus 로고    scopus 로고
    • AMoRe: An automated molecular replacement program package
    • DOI 10.1016/S0076-6879(97)76079-8
    • Navaza, J., and Saludijan, P. (1997) AMoRe: An automated molecular replacement program package. Methods Enzymol. 276, 581-594 (Pubitemid 27085624)
    • (1997) Methods in Enzymology , vol.276 , pp. 581-594
    • Navaza, J.1    Saludjian, P.2
  • 28
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992) Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 30
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • DOI 10.1016/S0076-6879(97)77018-6
    • Sheldrick, G. M., and Schneider, T. R. (1997) SHELXL: high-resolution refinement. Methods Enzymol. 277, 319-343 (Pubitemid 27390928)
    • (1997) Methods in Enzymology , vol.277 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 32
    • 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
  • 34
    • 0042011224 scopus 로고    scopus 로고
    • Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals
    • DOI 10.1110/ps.0350503
    • Kantardjieff, K. A., and Rupp, B. (2003) Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and proteinnucleic acid complex crystals. Protein Sci. 12, 1865-1871 (Pubitemid 37022809)
    • (2003) Protein Science , vol.12 , Issue.9 , pp. 1865-1871
    • Kantardjieff, K.A.1    Rupp, B.2
  • 35
    • 0013815214 scopus 로고
    • Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units
    • Ramakrishnan, C., and Ramachandran, G. N. (1965) Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units. Biophys. J. 5, 909-933
    • (1965) Biophys. J. , vol.5 , pp. 909-933
    • Ramakrishnan, C.1    Ramachandran, G.N.2
  • 37
    • 0014689979 scopus 로고
    • Role of a buried acid group in the mechanism of action of chymotrypsin
    • Blow, D. M., Birktoft, J. J., and Hartley, B. S. (1969) Role of a buried acid group in the mechanism of action of chymotrypsin. Nature 221, 337-340
    • (1969) Nature , vol.221 , pp. 337-340
    • Blow, D.M.1    Birktoft, J.J.2    Hartley, B.S.3
  • 39
    • 0026525805 scopus 로고
    • Histidine-aromatic interactions in barnase. Elevation of histidine Ka and contribution to protein stability
    • Loewenthal, R., Sancho, J., and Fersht, A. R. (1992) Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. J. Mol. Biol. 224, 759-770
    • (1992) J. Mol. Biol. , vol.224 , pp. 759-770
    • Loewenthal, R.1    Sancho, J.2    Fersht, A.R.3
  • 40
    • 33847799412 scopus 로고
    • Structure and mechanism of chymotrypsin
    • Blow, D. M. (1976) Structure and mechanism of chymotrypsin. Acc. Chem. Res. 9, 145-152
    • (1976) Acc. Chem. Res. , vol.9 , pp. 145-152
    • Blow, D.M.1
  • 41
    • 2642585575 scopus 로고    scopus 로고
    • Role of the 17 protein in proteolytic processing of vaccinia virus membrane and core components
    • DOI 10.1128/JVI.78.12.6335-6343.2004
    • Ansarah-Sobrinho, C., and Moss, B. (2004) Role of the I7 protein in proteolytic processing of vaccinia virus membrane and core components. J. Virol. 78, 6335-6343 (Pubitemid 38715932)
    • (2004) Journal of Virology , vol.78 , Issue.12 , pp. 6335-6343
    • Ansarah-Sobrinho, C.1    Moss, B.2
  • 42
    • 0035808469 scopus 로고    scopus 로고
    • African swine fever virus protease, a new viral member of the SUMO-1-specific protease family
    • DOI 10.1074/jbc.M006844200
    • Andrés, G., Alejo, A., Simón-Mateo, C., and Salas, M. L. (2001) African swine fever virus protease, a new viral member of the SUMO-1-specific protease family. J. Biol. Chem. 276, 780-787 (Pubitemid 32050378)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.1 , pp. 780-787
    • Andres, G.1    Alejo, A.2    Simon-Mateo, C.3    Salas, M.L.4
  • 44
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cellcycle progression in yeast
    • Li, S.-J., and Hochstrasser, M. (1999) A new protease required for cellcycle progression in yeast. Nature 398, 246-251
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.-J.1    Hochstrasser, M.2
  • 45
    • 33744457909 scopus 로고    scopus 로고
    • Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation
    • DOI 10.1126/science.1126867
    • Mukherjee, S., Keitany, G., Li, Y., Wang, Y., Ball, H. L., Goldsmith, E. J., and Orth, K. (2006) Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. Science 312, 1211-1214 (Pubitemid 43801146)
    • (2006) Science , vol.312 , Issue.5777 , pp. 1211-1214
    • Mukherjee, S.1    Keitany, G.2    Li, Y.3    Wang, Y.4    Ball, H.L.5    Goldsmith, E.J.6    Orth, K.7
  • 46
    • 84872701041 scopus 로고    scopus 로고
    • Regulation of a viral proteinase by a peptide and DNA in one-dimensional space. I. Binding to DNA and to hexon of the precursor to protein VI, pVI, of human adenovirus
    • Graziano, V., McGrath, W. J., Suomalainen, M., Greber, U.F., Freimuth, P., Blainey, P.C., Luo, G., Xie, X.S., and Mangel, W.F. (2012) Regulation of a viral proteinase by a peptide and DNA in one-dimensional space. I. Binding to DNA and to hexon of the precursor to protein VI, pVI, of human adenovirus. J. Biol. Chem. 287, 2059-2067
    • (2012) J. Biol. Chem. , vol.287 , pp. 2059-2067
    • Graziano, V.1    McGrath, W.J.2    Suomalainen, M.3    Greber, U.F.4    Freimuth, P.5    Blainey, P.C.6    Luo, G.7    Xie, X.S.8    Mangel, W.F.9
  • 47
    • 84872699552 scopus 로고    scopus 로고
    • Regulation of a viral proteinase by a peptide and DNA in one-dimensional space. II. Adenovirus proteinase is activated in an unusual one-dimensional biochemical reaction
    • Graziano, V., Luo, G. Blainey, P.C., Pérez-Berná, A. J., McGrath, W. J., Flint, S. J., San Martín, C., Xie, X.S., and Mangel, W.F. (2012) Regulation of a viral proteinase by a peptide and DNA in one-dimensional space. II. Adenovirus proteinase is activated in an unusual one-dimensional biochemical reaction. J. Biol. Chem. 287, 2068-2080
    • (2012) J. Biol. Chem. , vol.287 , pp. 2068-2080
    • Graziano, V.1    Luo Blainey G, P.C.2    Pérez-Berná, A.J.3    McGrath, W.J.4    Flint, S.J.5    San Martín, C.6    Xie, X.S.7    Mangel, W.F.8
  • 48
    • 84872726119 scopus 로고    scopus 로고
    • Regulation of a viral proteinase by a peptide and DNA in one-dimensional space. IV. Viral proteinase slides along DNA to locate and process its substrates
    • Blainey, P. C., Graziano, V., Pérez-Berná, A. J., McGrath, W. J., Flint, S. J., San Martín, C., Xie, X. S., and Mangel. W. F. (2012) Regulation of a viral proteinase by a peptide and DNA in one-dimensional space. IV. Viral proteinase slides along DNA to locate and process its substrates. J. Biol. Chem. 287, 2092-2102
    • (2012) J. Biol. Chem. , vol.287 , pp. 2092-2102
    • Blainey, P.C.1    Graziano, V.2    Pérez-Berná, A.J.3    McGrath, W.J.4    Flint, S.J.5    San Martín, C.6    Xie, X.S.7    Mangel, W.F.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.