메뉴 건너뛰기




Volumn 141, Issue 2, 2003, Pages 171-178

Crystal structure of pokeweed antiviral protein with well-defined sugars from seeds at 1.8 Å resolution

Author keywords

Crystal structure; N Acetylglucosamine; Pokeweed antiviral protein; Ribosome inactivating protein

Indexed keywords

ASPARAGINE; N ACETYLGLUCOSAMINE; POKEWEED ANTIVIRUS PROTEIN; POLYPEPTIDE; SUGAR;

EID: 0037291290     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1047-8477(02)00580-4     Document Type: Article
Times cited : (15)

References (38)
  • 1
    • 0027968488 scopus 로고
    • X-ray structure of a pokeweed antiviral protein, coded by a new genomic clone, at 0.23 nm resolution
    • Ago H., Kataoka J., Tsuge H., Habuka N., Inagaki E., Noma M., Miyano M. X-ray structure of a pokeweed antiviral protein, coded by a new genomic clone, at 0.23. nm resolution Eur. J. Biochem. 225:1994;369-374.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 369-374
    • Ago, H.1    Kataoka, J.2    Tsuge, H.3    Habuka, N.4    Inagaki, E.5    Noma, M.6    Miyano, M.7
  • 2
    • 0033607003 scopus 로고    scopus 로고
    • Placement of protein and RNA structures into a 5 Å resolution map of the 50S ribosome subunit
    • Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A. Placement of protein and RNA structures into a 5. Å resolution map of the 50S ribosome subunit Nature. 400:1999;841-847.
    • (1999) Nature , vol.400 , pp. 841-847
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Capel, M.4    Moore, P.B.5    Steitz, T.A.6
  • 3
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., Nissen P., Hansen J., Moor P.B., Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4. Å resolution Science. 289:2000;905-919.
    • (2000) Science , vol.289 , pp. 905-919
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moor, P.B.4    Steitz, T.A.5
  • 4
    • 0020123674 scopus 로고
    • Purification and partial characterization of another form of the antiviral protein from the seeds of Phytolacca americana L (pokeweed)
    • Barbieri L., Aron G.M., Irvin J.D., Stirpe F. Purification and partial characterization of another form of the antiviral protein from the seeds of Phytolacca americana L (pokeweed). Biochem. J. 203:1982;55-59.
    • (1982) Biochem. J. , vol.203 , pp. 55-59
    • Barbieri, L.1    Aron, G.M.2    Irvin, J.D.3    Stirpe, F.4
  • 6
    • 0030746170 scopus 로고    scopus 로고
    • Polynucleotide: Adenosine glycosidase activity of ribosome-inactivating proteins: Effect on DNA, RNA and poly(A)
    • Barbieri L., Valbonesi P., Bonora E., Gorini P., Bolognesi A., Stirpe F. Polynucleotide: adenosine glycosidase activity of ribosome-inactivating proteins: effect on DNA, RNA and poly(A). Nucleic Acids Res. 25:1997;518-522.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 518-522
    • Barbieri, L.1    Valbonesi, P.2    Bonora, E.3    Gorini, P.4    Bolognesi, A.5    Stirpe, F.6
  • 8
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger A.T., Kuriyan J., Karplus M. Crystallographic R factor refinement by molecular dynamics. Science. 235:1987;458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 10
    • 0030022569 scopus 로고    scopus 로고
    • Report of a workshop on the use of statistical validators in protein X-ray crystallography
    • Dodson E., Kleywegt G.J., Wilson K. Report of a workshop on the use of statistical validators in protein X-ray crystallography. Acta Crystallogr. D. 52:1996;228-234.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 228-234
    • Dodson, E.1    Kleywegt, G.J.2    Wilson, K.3
  • 11
    • 0025863844 scopus 로고
    • Ribosomal RNA identity elements for ricin A-chain recognition and catalysis
    • Endo Y., Gluck A., Wool I.G. Ribosomal RNA identity elements for ricin A-chain recognition and catalysis. J. Mol. Biol. 221:1991;193-207.
    • (1991) J. Mol. Biol. , vol.221 , pp. 193-207
    • Endo, Y.1    Gluck, A.2    Wool, I.G.3
  • 12
    • 0002193613 scopus 로고
    • The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography
    • Higashi T. The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography. J. Appl. Crystallogr. 22:1989;9-18.
    • (1989) J. Appl. Crystallogr. , vol.22 , pp. 9-18
    • Higashi, T.1
  • 13
    • 0036185617 scopus 로고    scopus 로고
    • Genomic clones encoding two isoforms of pokeweed antiviral protein in seeds (PAP-S1 and S2) and the N-glycosidase activities of their recombinant proteins on ribosomes and DNA in comparison with other isoforms
    • Honjo E., Dong D., Motoshima H., Watanabe K. Genomic clones encoding two isoforms of pokeweed antiviral protein in seeds (PAP-S1 and S2) and the N-glycosidase activities of their recombinant proteins on ribosomes and DNA in comparison with other isoforms. J. Biochem. 131:2002;225-231.
    • (2002) J. Biochem. , vol.131 , pp. 225-231
    • Honjo, E.1    Dong, D.2    Motoshima, H.3    Watanabe, K.4
  • 14
    • 0029032663 scopus 로고
    • Studies on crystal structures, active-center geometry and depurinating mechanism of two ribosome-inactivating proteins
    • Huang Q., Liu S., Tang Y., Jin S., Wang Y. Studies on crystal structures, active-center geometry and depurinating mechanism of two ribosome-inactivating proteins. Biochem. J. 309:1995;285-298.
    • (1995) Biochem. J. , vol.309 , pp. 285-298
    • Huang, Q.1    Liu, S.2    Tang, Y.3    Jin, S.4    Wang, Y.5
  • 15
    • 0033524919 scopus 로고    scopus 로고
    • Pokeweed antiviral protein accesses ribosomes by binding to L3
    • Hudak K.A., Diman J.D., Tumer N.E. Pokeweed antiviral protein accesses ribosomes by binding to L3. J. Biol. Chem. 274:1999;3859-3864.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3859-3864
    • Hudak, K.A.1    Diman, J.D.2    Tumer, N.E.3
  • 16
    • 0016764387 scopus 로고
    • Purification and partial characterization of the antiviral protein from Phytolacca americana which inhibits eukaryotic protein synthesis
    • Irvin J.D. Purification and partial characterization of the antiviral protein from Phytolacca americana which inhibits eukaryotic protein synthesis. Arch. Biochem. Biophys. 169:1975;522-528.
    • (1975) Arch. Biochem. Biophys. , vol.169 , pp. 522-528
    • Irvin, J.D.1
  • 17
    • 0019258945 scopus 로고
    • Purification and properties of a second antiviral protein from Phytolacca americana which inactivates eukaryotic ribosomes
    • Irvin J.D., Kelly T., Robertus J.D. Purification and properties of a second antiviral protein from Phytolacca americana which inactivates eukaryotic ribosomes. Arch. Biochem. Biophys. 200:1980;418-425.
    • (1980) Arch. Biochem. Biophys. , vol.200 , pp. 418-425
    • Irvin, J.D.1    Kelly, T.2    Robertus, J.D.3
  • 18
    • 0026161808 scopus 로고
    • N-Acetyl-D-glucosamine-asparagine structure in ribosome-inactivating proteins from the seeds of Luffa cylindrica and Phytolacca americana
    • Islam M.R., Kung S.S., Kimura Y., Funatsu G. N-Acetyl-D-glucosamine-asparagine structure in ribosome-inactivating proteins from the seeds of Luffa cylindrica and Phytolacca americana. Agric. Biol. Chem. 55:1991;1375-1381.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1375-1381
    • Islam, M.R.1    Kung, S.S.2    Kimura, Y.3    Funatsu, G.4
  • 19
    • 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., Kjeldgaard M. 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
  • 20
    • 0027015895 scopus 로고
    • Isolation and analysis of a genomic clone encoding a pokeweed antiviral protein
    • Kataoka J., Habuka N., Masuta C., Miyano M., Koiwai A. Isolation and analysis of a genomic clone encoding a pokeweed antiviral protein. Plant Mol. Biol. 20:1992;879-886.
    • (1992) Plant Mol. Biol. , vol.20 , pp. 879-886
    • Kataoka, J.1    Habuka, N.2    Masuta, C.3    Miyano, M.4    Koiwai, A.5
  • 21
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination: Applications of the free R value
    • Kleywegt G.J., Brünger A.T. Checking your imagination: applications of the free R value. Structure. 4:1996;879-904.
    • (1996) Structure , vol.4 , pp. 879-904
    • Kleywegt, G.J.1    Brünger, A.T.2
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0032822087 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of the structural basis for the interaction of pokeweed antiviral protein with its active site inhibitor and ribosomal RNA analogs
    • Kurinov I.V., Myers D.E., Irvin J.D., Uckun F.M. X-ray crystallographic analysis of the structural basis for the interaction of pokeweed antiviral protein with its active site inhibitor and ribosomal RNA analogs. Protein Sci. 8:1999;1722-1765.
    • (1999) Protein Sci. , vol.8 , pp. 1722-1765
    • Kurinov, I.V.1    Myers, D.E.2    Irvin, J.D.3    Uckun, F.M.4
  • 24
    • 0032725662 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of the structural basis for the interaction of pokeweed antiviral protein with guanine residues of ribosomal RNA
    • Kurinov I.V., Rajamohan T.K., Venkatachalam T.K., Uckun F.M. X-ray crystallographic analysis of the structural basis for the interaction of pokeweed antiviral protein with guanine residues of ribosomal RNA. Protein Sci. 8:1999;2399-2405.
    • (1999) Protein Sci. , vol.8 , pp. 2399-2405
    • Kurinov, I.V.1    Rajamohan, T.K.2    Venkatachalam, T.K.3    Uckun, F.M.4
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereo chemical quality of protein structure
    • Laskowski R.A., MacArthur M.W., Moss D.S., Thorton J.M PROCHECK: a program to check the stereo chemical quality of protein structure. J. Appl. Crystallogr. 28:1993;283-291.
    • (1993) J. Appl. Crystallogr. , vol.28 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thorton J.M4
  • 26
    • 0031936812 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analyses of pokeweed antiviral protein from seeds
    • Li H.M., Zeng Z.H., Hu Z., Wang D.C. Crystallization and preliminary crystallographic analyses of pokeweed antiviral protein from seeds. Acta Crystallogr. D. 54:1998;137-139.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 137-139
    • Li, H.M.1    Zeng, Z.H.2    Hu, Z.3    Wang, D.C.4
  • 28
    • 0026469648 scopus 로고
    • X-ray analysis of substrate analogs in the ricin A-chain active site
    • Monzingo A.F., Robertus J.D. X-ray analysis of substrate analogs in the ricin A-chain active site. J. Mol. Biol. 227:1992;1136-1145.
    • (1992) J. Mol. Biol. , vol.227 , pp. 1136-1145
    • Monzingo, A.F.1    Robertus, J.D.2
  • 29
    • 84920325457 scopus 로고
    • AmoRe - An automated package for molecular replacement
    • Navaza J. AmoRe - an automated package for molecular replacement. Acta Crystallogr. A. 50:1994;157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 34
    • 0000525517 scopus 로고
    • A focusing Weissenburg camera with multi-layer-line screens for macromolecular crystallography
    • Sakabe N. A focusing Weissenburg camera with multi-layer-line screens for macromolecular crystallography. J. Appl. Crystallog. 16:1989;542-547.
    • (1989) J. Appl. Crystallog. , vol.16 , pp. 542-547
    • Sakabe, N.1
  • 35
    • 14744291476 scopus 로고
    • Ribosome-inactivating proteins from plants: Present status and future prospects
    • Stirpe F., Barbieri L., Battelli M.G., Soria M., Lappi D.A. Ribosome-inactivating proteins from plants: present status and future prospects. Biotechnology. 10:1992;405-412.
    • (1992) Biotechnology , vol.10 , pp. 405-412
    • Stirpe, F.1    Barbieri, L.2    Battelli, M.G.3    Soria, M.4    Lappi, D.A.5
  • 37
    • 0033566020 scopus 로고    scopus 로고
    • Glycoproteins: Glycan presentation and protein-fold stability
    • Wormald M.R., Dwek R.A. Glycoproteins: glycan presentation and protein-fold stability. Structure. 7:1999;R155-R160.
    • (1999) Structure , vol.7
    • Wormald, M.R.1    Dwek, R.A.2
  • 38
    • 0012136557 scopus 로고
    • Preparation of the antiviral protein from pokeweed seeds and assay of its toxicity
    • Zhu X., Hu Z. Preparation of the antiviral protein from pokeweed seeds and assay of its toxicity. Acta Bot. Yunnanica. 11:1989;440-448.
    • (1989) Acta Bot. Yunnanica , vol.11 , pp. 440-448
    • Zhu, X.1    Hu, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.