메뉴 건너뛰기




Volumn 80, Issue 15, 2006, Pages 7636-7644

Structure of A197 from Sulfolobus turreted icosahedral virus: A crenarchaeal viral glycosyltransferase exhibiting the GT-A fold

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; DOUBLE STRANDED DNA; GLYCOSYLTRANSFERASE; PROTEOME;

EID: 33746210125     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00567-06     Document Type: Article
Times cited : (48)

References (67)
  • 2
    • 0141677902 scopus 로고    scopus 로고
    • Constrained synthesis of cobalt oxide nanomaterials in the 12-subunit protein cage from Listeria innocua
    • Allen, M., D. Willits, M. Young, and T. Douglas. 2003. Constrained synthesis of cobalt oxide nanomaterials in the 12-subunit protein cage from Listeria innocua. Inorg. Chem. 42:6300-6305.
    • (2003) Inorg. Chem. , vol.42 , pp. 6300-6305
    • Allen, M.1    Willits, D.2    Young, M.3    Douglas, T.4
  • 5
  • 6
    • 9744228738 scopus 로고    scopus 로고
    • Docs common architecture reveal a viral lineage spanning alt three domains of life?
    • Benson, S. D., J. K. H. Baniford, D. H. Bamford, and R. M. Burnett. 2004. Docs common architecture reveal a viral lineage spanning alt three domains of life? Mol. Cell 16:673-685.
    • (2004) Mol. Cell , vol.16 , pp. 673-685
    • Benson, S.D.1    Baniford, J.K.H.2    Bamford, D.H.3    Burnett, R.M.4
  • 7
    • 0033578669 scopus 로고    scopus 로고
    • Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures
    • Benson, S. D., J. K. H. Bamford, D. H. Bamford, and R. M. Burnett. 1999. Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures. Cell 98:825-833.
    • (1999) Cell , vol.98 , pp. 825-833
    • Benson, S.D.1    Bamford, J.K.H.2    Bamford, D.H.3    Burnett, R.M.4
  • 8
    • 0242300042 scopus 로고    scopus 로고
    • AFV1, a novel virus infecting hyperthermophilic Archaea of the genus Acidianus
    • Bettstetter, M., X. Peng, R. A. Garrett, and D. Prangishvili. 2003. AFV1, a novel virus infecting hyperthermophilic Archaea of the genus Acidianus. Virology 315:68-79.
    • (2003) Virology , vol.315 , pp. 68-79
    • Bettstetter, M.1    Peng, X.2    Garrett, R.A.3    Prangishvili, D.4
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0002815512 scopus 로고
    • D-glyceraldehyde-3-phosphate dehydrogenase: Three-dimensional structure and evolutionary significance
    • Buehner, M., G. C. Ford, D. Moras, K. W. Olsen, and M. G. Rossmann. 1973. D-glyceraldehyde-3-phosphate dehydrogenase: three-dimensional structure and evolutionary significance. Proc. Natl. Acad. Sci. USA 70:3052-3054.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 3052-3054
    • Buehner, M.1    Ford, G.C.2    Moras, D.3    Olsen, K.W.4    Rossmann, M.G.5
  • 12
    • 0033580656 scopus 로고    scopus 로고
    • Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms
    • 11a. Charnock, S. J., and G. J. Davies. 1999. Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms. Biochemistry 38:6380-6385.
    • (1999) Biochemistry , vol.38 , pp. 6380-6385
    • Charnock, S.J.1    Davies, G.J.2
  • 15
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho, P. M., E. Deleury, G. J. Davies, and B. Henrissat. 2003. An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 328:307-317.
    • (2003) J. Mol. Biol. , vol.328 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 17
    • 27944434246 scopus 로고    scopus 로고
    • Recent structural insights into the expanding world of carbohydrate-active enzymes
    • Davies, G. J., T. M. Gloster, and B. Henrissat. 2005. Recent structural insights into the expanding world of carbohydrate-active enzymes. Curr. Opin. Struct. Biol. 15:637-645.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 637-645
    • Davies, G.J.1    Gloster, T.M.2    Henrissat, B.3
  • 19
    • 24944463449 scopus 로고    scopus 로고
    • Posttranslational protein modification in Archaea
    • Eichler, J., and M. W. W. Adams. 2005. Posttranslational protein modification in Archaea. Microbiol. Mol. Biol. Rev. 69:393-425.
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 393-425
    • Eichler, J.1    Adams, M.W.W.2
  • 21
    • 0242319704 scopus 로고    scopus 로고
    • Fold recognition analysis of glycosyltransferase families: Further members of structural superfamilies
    • Franco, O. L., and D. J. Rigden. 2003. Fold recognition analysis of glycosyltransferase families: further members of structural superfamilies. Glycobiology 13:707-712.
    • (2003) Glycobiology , vol.13 , pp. 707-712
    • Franco, O.L.1    Rigden, D.J.2
  • 22
    • 0033168184 scopus 로고    scopus 로고
    • Crystal structures of the bovine β4 galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
    • Gastinel, L., C. Cambillau, and Y. Bourne. 1999. Crystal structures of the bovine β4 galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose. EMBO J. 18:3546-3557.
    • (1999) EMBO J. , vol.18 , pp. 3546-3557
    • Gastinel, L.1    Cambillau, C.2    Bourne, Y.3
  • 24
    • 0035811885 scopus 로고    scopus 로고
    • Molecular and genetic evidence for a virus-encoded glycosyltransferase involved in protein glycosylation
    • Graves, M. V., C. T. Bernadt, R. Cerny, and J. L. Van Etten. 2001. Molecular and genetic evidence for a virus-encoded glycosyltransferase involved in protein glycosylation. Virology 285:332-345.
    • (2001) Virology , vol.285 , pp. 332-345
    • Graves, M.V.1    Bernadt, C.T.2    Cerny, R.3    Van Etten, J.L.4
  • 25
    • 18944393962 scopus 로고    scopus 로고
    • Structure and genome organization of AFV2, a novel archaeal lipothrixvirus with unusual terminal and core structures
    • Haring, M., G. Vestergaard, K. Brugger, R. Rachel, R. A. Garrett, and D. Prangishvili. 2005. Structure and genome organization of AFV2, a novel archaeal lipothrixvirus with unusual terminal and core structures. J. Bacteriol. 187:3855-3858.
    • (2005) J. Bacteriol. , vol.187 , pp. 3855-3858
    • Haring, M.1    Vestergaard, G.2    Brugger, K.3    Rachel, R.4    Garrett, R.A.5    Prangishvili, D.6
  • 27
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L., and C. Sander. 1993. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233:123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J. Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. Sect. A 47:110-119.
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch, W. 1976. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. Sect. A 32:922-923.
    • (1976) Acta Crystallogr. Sect. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 30
    • 30044450170 scopus 로고    scopus 로고
    • Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses
    • Khayat, R., L. Tang, E. T. Larson, C. M. Lawrence, M. Young, and J. E. Johnson. 2005. Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses. Proc. Natl. Acad. Sci. USA 102:18944-18949.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18944-18949
    • Khayat, R.1    Tang, L.2    Larson, E.T.3    Lawrence, C.M.4    Young, M.5    Johnson, J.E.6
  • 31
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • Kleywegt, G. 1996. Use of non-crystallographic symmetry in protein structure refinement. Acta Crystallogr Sect. D Biol. Crystallogr. 52:842-857.
    • (1996) Acta Crystallogr Sect. D Biol. Crystallogr. , vol.52 , pp. 842-857
    • Kleywegt, G.1
  • 32
    • 20244382943 scopus 로고    scopus 로고
    • Structure of D-63 from sulfolohus spindle-shaped virus 1: Surface properties of the dimeric four-helix bundle suggest an adaptor protein function
    • Kraft, P., D. Kummel, A. Oeckinghaus, G. H. Gauss, B. Wiedenheft, M. Young, and C. M. Lawrence. 2004. Structure of D-63 from sulfolohus spindle-shaped virus 1: surface properties of the dimeric four-helix bundle suggest an adaptor protein function. J. Virol. 78:7438-7442.
    • (2004) J. Virol. , vol.78 , pp. 7438-7442
    • Kraft, P.1    Kummel, D.2    Oeckinghaus, A.3    Gauss, G.H.4    Wiedenheft, B.5    Young, M.6    Lawrence, C.M.7
  • 34
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. MacArthur, D. S. Moss, and J. M. Thornton. 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
    • 0031687653 scopus 로고    scopus 로고
    • Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design
    • Liang, J., H. Edelshrunner, and C. Woodward. 1998. Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design. Protein Sci. 7:1884-1897.
    • (1998) Protein Sci. , vol.7 , pp. 1884-1897
    • Liang, J.1    Edelshrunner, H.2    Woodward, C.3
  • 36
    • 33746210122 scopus 로고    scopus 로고
    • Characterization of the archaeal thermophile Sulfolobus turreted icosahedral virus validates an evolutionary link among double-stranded DNA viruses from all domains of life
    • Maaty, W. S. A., A. C. Ortmann, M. Dlakić, K. Schulstad, J. Hilmer, L. Liepold, B. Weidenheft, T. Douglas, M. Young, and B. Bothner. 2006. Characterization of the archaeal thermophile Sulfolobus turreted icosahedral virus validates an evolutionary link among double-stranded DNA viruses from all domains of life. J. Virol. 80:7625-7635.
    • (2006) J. Virol. , vol.80 , pp. 7625-7635
    • Maaty, W.S.A.1    Ortmann, A.C.2    Dlakić, M.3    Schulstad, K.4    Hilmer, J.5    Liepold, L.6    Weidenheft, B.7    Douglas, T.8    Young, M.9    Bothner, B.10
  • 37
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: Protein domain annotations on the fly
    • Marchler-Bauer, A., and S. H. Bryant. 2004. CD-Search: protein domain annotations on the fly. Nucleic Acids Res. 32:W327-W331.
    • (2004) Nucleic Acids Res. , vol.32
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 39
    • 0026662396 scopus 로고
    • Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles
    • Mengele, R., and M. Sumper. 1992. Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles. J. Biol. Chem. 267:8182-8185.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8182-8185
    • Mengele, R.1    Sumper, M.2
  • 44
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Macromol. Crystallogr. 276:307-326.
    • (1997) Macromol. Crystallogr. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 45
    • 23844520061 scopus 로고    scopus 로고
    • A molecular viewer for the analysis of TLS rigid-body motion in macromolecules
    • Painter, J., and E. A. Merritt. 2005. A molecular viewer for the analysis of TLS rigid-body motion in macromolecules. Acta Crystallogr. Sect. D Biol. Crystallgr. 61:465-471.
    • (2005) Acta Crystallogr. Sect. D Biol. Crystallgr. , vol.61 , pp. 465-471
    • Painter, J.1    Merritt, E.A.2
  • 46
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J., and E. A. Merritt. 2006. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. Sect. D Biol. Crystallgr. 62:439-450.
    • (2006) Acta Crystallogr. Sect. D Biol. Crystallgr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 47
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter, J., and E. A. Merritt. 2006. TLSMD web server for the generation of multi-group TLS models. J. Appl. Crystallogr. 39:109-111.
    • (2006) J. Appl. Crystallogr. , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 48
    • 0037077202 scopus 로고    scopus 로고
    • Crystal structure of β1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA
    • Pedersen, L. C., T. A. Darden, and M. Negishi. 2002. Crystal structure of β1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA. J. Biol. Chem. 277:21869-21873.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21869-21873
    • Pedersen, L.C.1    Darden, T.A.2    Negishi, M.3
  • 49
    • 0034602394 scopus 로고    scopus 로고
    • Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I
    • Pedersen, L. C., K. Tsuchida, H. Kitagawa, K. Sugahara, T. A. Darden, and M. Negishi. 2000. Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I. J. Biol. Chem. 275:34580-34585.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34580-34585
    • Pedersen, L.C.1    Tsuchida, K.2    Kitagawa, H.3    Sugahara, K.4    Darden, T.A.5    Negishi, M.6
  • 50
    • 0035694680 scopus 로고    scopus 로고
    • Sequences and replication of genomes of the archaeal rudiviruses SIRV1 and SIRV2: Relationships to the archaeal lipothrixvirus SIFV and some eukaryal viruses
    • Peng, X., H. Blum, Q. She, S. Mallok, K. Brugger, R. A. Garrett, W. Zillig, and D. Prangishvili. 2001. Sequences and replication of genomes of the archaeal rudiviruses SIRV1 and SIRV2: relationships to the archaeal lipothrixvirus SIFV and some eukaryal viruses. Virology 291:226-234.
    • (2001) Virology , vol.291 , pp. 226-234
    • Peng, X.1    Blum, H.2    She, Q.3    Mallok, S.4    Brugger, K.5    Garrett, R.A.6    Zillig, W.7    Prangishvili, D.8
  • 51
    • 6344269355 scopus 로고    scopus 로고
    • Multiple variants of the archaeal DNA rudivirus SIRV1 in a single host and a novel mechanism of genomic variation
    • Peng, X., A. Kessler, H. Phan, R. A. Garrett, and D. Prangishvili. 2004. Multiple variants of the archaeal DNA rudivirus SIRV1 in a single host and a novel mechanism of genomic variation. Mol. Microbiol. 54:366-375.
    • (2004) Mol. Microbiol. , vol.54 , pp. 366-375
    • Peng, X.1    Kessler, A.2    Phan, H.3    Garrett, R.A.4    Prangishvili, D.5
  • 52
    • 3242878412 scopus 로고    scopus 로고
    • 3DCoffee@igs: A web server for combining sequences and structures into a multiple sequence alignment
    • Poirot, O., K. Suhre, C. Abergel, E. O'Toole, and C. Notredame. 2004. 3DCoffee@igs: a web server for combining sequences and structures into a multiple sequence alignment. Nucleic Acids Res. 32:W37-W40.
    • (2004) Nucleic Acids Res. , vol.32
    • Poirot, O.1    Suhre, K.2    Abergel, C.3    O'Toole, E.4    Notredame, C.5
  • 53
    • 27144541842 scopus 로고    scopus 로고
    • Viruses of hyperthermophilic crenarchaea
    • Prangishvili, D., and R. A. Garrett. 2005. Viruses of hyperthermophilic crenarchaea. Trends Microbiol. 13:535-542.
    • (2005) Trends Microbiol. , vol.13 , pp. 535-542
    • Prangishvili, D.1    Garrett, R.A.2
  • 57
    • 0042890357 scopus 로고    scopus 로고
    • Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution X-ray crystallographic, molecular modeling, and sequence-based methods
    • Rux, J. J., P. R. Kuser, and R. M. Burnett. 2003. Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution X-ray crystallographic, molecular modeling, and sequence-based methods. J. Virol. 77: 9553-9566.
    • (2003) J. Virol. , vol.77 , pp. 9553-9566
    • Rux, J.J.1    Kuser, P.R.2    Burnett, R.M.3
  • 58
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model-building by template-matching and iterative fragment extension
    • Terwilliger, T. C. 2002. Automated main-chain model-building by template-matching and iterative fragment extension. Acta Crystallogr. Sect. D Biol. Crystallgr. 59:34-44.
    • (2002) Acta Crystallogr. Sect. D Biol. Crystallgr. , vol.59 , pp. 34-44
    • Terwilliger, T.C.1
  • 61
    • 0033026970 scopus 로고    scopus 로고
    • Eflicient expression, purification and crystallisation of two hyperthermostable enzymes of histidine biosynthesis
    • Thoma, R., G. Ohmolova, D. A. Lang, M. Schwander, P. Jenö, R. Sterner, and M. Wilmanns. 1999. Eflicient expression, purification and crystallisation of two hyperthermostable enzymes of histidine biosynthesis. FEBS Lett. 454:1-6.
    • (1999) FEBS Lett. , vol.454 , pp. 1-6
    • Thoma, R.1    Ohmolova, G.2    Lang, D.A.3    Schwander, M.4    Jenö, P.5    Sterner, R.6    Wilmanns, M.7
  • 62
    • 0033787822 scopus 로고    scopus 로고
    • Glycosyltransferase structure and mechanism
    • Unligil, U. M., and J. M. Rini. 2000. Glycosyltransferase structure and mechanism. Curr. Opin. Struct. Biol. 10:510-517.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 510-517
    • Unligil, U.M.1    Rini, J.M.2
  • 63
    • 0034675845 scopus 로고    scopus 로고
    • X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: Catalytic mechanism and a new protein superfamily
    • Unligil, U. M., S. Zhou, S. Yuwaraj, M. Sarkar, H. Schachter, and J. M. Rini. 2000. X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily. EMBO J. 19:5269-5280.
    • (2000) EMBO J. , vol.19 , pp. 5269-5280
    • Unligil, U.M.1    Zhou, S.2    Yuwaraj, S.3    Sarkar, M.4    Schachter, H.5    Rini, J.M.6
  • 65
    • 0029904281 scopus 로고    scopus 로고
    • Influence of the carbohydrate moiety on the stability of glycoproteins
    • Wang, C., M. Eufemi, C. Turano, and A. Giartosio. 1996. Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry 35:7299-7307.
    • (1996) Biochemistry , vol.35 , pp. 7299-7307
    • Wang, C.1    Eufemi, M.2    Turano, C.3    Giartosio, A.4
  • 66
    • 21644445703 scopus 로고    scopus 로고
    • Sulfolobus tengchongensis spindle-shaped virus STSV1: Virus-host interactions and genomic features
    • Xiang, X., L. Chen, X. Huang, Y. Luo, Q. She, and L. Huang. 2005. Sulfolobus tengchongensis spindle-shaped virus STSV1: virus-host interactions and genomic features. J. Virol. 79:8677-8686.
    • (2005) J. Virol. , vol.79 , pp. 8677-8686
    • Xiang, X.1    Chen, L.2    Huang, X.3    Luo, Y.4    She, Q.5    Huang, L.6
  • 67
    • 0033625671 scopus 로고    scopus 로고
    • 558/566 from the archaeon Sulfolobus acidocaldarius has a unique Asn-linked highly branched hexasaccharide chain containing 6-sulfoquinovose
    • 558/566 from the archaeon Sulfolobus acidocaldarius has a unique Asn-linked highly branched hexasaccharide chain containing 6-sulfoquinovose. Eur. J. Biochem. 267:4144-4149.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4144-4149
    • Zahringer, U.1    Moll, H.2    Hettmann, T.3    Knirel, Y.A.4    Schafer, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.