메뉴 건너뛰기




Volumn 375, Issue 1, 2008, Pages 190-196

Structure of recombinant capsids formed by the β-annulus deletion mutant - rCP (Δ48-59) of Sesbania mosaic virus

Author keywords

annulus; Coat protein; Sesbania mosaic virus; Virus assembly; X ray crystallography

Indexed keywords

COAT PROTEIN;

EID: 42749093687     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2008.01.023     Document Type: Article
Times cited : (12)

References (34)
  • 4
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions
    • Cohen G.E. ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions. J. Appl. Crystallogr. 1997 (1997) 1160-1161
    • (1997) J. Appl. Crystallogr. , vol.1997 , pp. 1160-1161
    • Cohen, G.E.1
  • 6
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet P., Robert X., and Courcelle E. ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res. 31 (2003) 3320-3323
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 7
    • 0023054002 scopus 로고
    • Structure and assembly of turnip crinkle virus. I. X-ray crystallographic structure analysis at 3.2 Å resolution
    • Hogle J.M., Maeda A., and Harrison S.C. Structure and assembly of turnip crinkle virus. I. X-ray crystallographic structure analysis at 3.2 Å resolution. J. Mol. Biol. 191 (1986) 625-638
    • (1986) J. Mol. Biol. , vol.191 , pp. 625-638
    • Hogle, J.M.1    Maeda, A.2    Harrison, S.C.3
  • 8
    • 33644641677 scopus 로고    scopus 로고
    • Characterization of polymorphism displayed by the coat protein mutants of tomato bushy stunt virus
    • Hsu C., Singh P., Ochoa W., Manayani D.J., Manchester M., Schneemann A., and Reddy V.S. Characterization of polymorphism displayed by the coat protein mutants of tomato bushy stunt virus. Virology 349 (2006) 222-229
    • (2006) Virology , vol.349 , pp. 222-229
    • Hsu, C.1    Singh, P.2    Ochoa, W.3    Manayani, D.J.4    Manchester, M.5    Schneemann, A.6    Reddy, V.S.7
  • 9
    • 33744909568 scopus 로고    scopus 로고
    • Evaluation of the roles of specific regions of the Cucumber necrosis virus coat protein in particle accumulation and fungus transmission
    • Hui E., and Rochon D. Evaluation of the roles of specific regions of the Cucumber necrosis virus coat protein in particle accumulation and fungus transmission. J. Virol. 80 (2006) 5968-5975
    • (2006) J. Virol. , vol.80 , pp. 5968-5975
    • Hui, E.1    Rochon, D.2
  • 10
    • 0031588020 scopus 로고    scopus 로고
    • Quasi-equivalent viruses: a paradigm for protein assemblies
    • Johnson J.E., and Speir J.A. Quasi-equivalent viruses: a paradigm for protein assemblies. J. Mol. Biol. 269 (1997) 665-675
    • (1997) J. Mol. Biol. , vol.269 , pp. 665-675
    • Johnson, J.E.1    Speir, J.A.2
  • 11
    • 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., and 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
  • 12
    • 1842635576 scopus 로고    scopus 로고
    • Evidence that vector transmission of a plant virus requires conformational change in virus particles
    • Kakani K., Reade R., and Rochon D. Evidence that vector transmission of a plant virus requires conformational change in virus particles. J. Mol. Biol. 338 (2004) 507-517
    • (2004) J. Mol. Biol. , vol.338 , pp. 507-517
    • Kakani, K.1    Reade, R.2    Rochon, D.3
  • 13
    • 1642487718 scopus 로고    scopus 로고
    • Structure of Cowpea mottle virus: a consensus in the genus Carmovirus
    • Ke J., Schmidt T., Chase E., Bozarth R.F., and Smith T.J. Structure of Cowpea mottle virus: a consensus in the genus Carmovirus. Virology 321 (2004) 349-358
    • (2004) Virology , vol.321 , pp. 349-358
    • Ke, J.1    Schmidt, T.2    Chase, E.3    Bozarth, R.F.4    Smith, T.J.5
  • 15
    • 0033598741 scopus 로고    scopus 로고
    • RNA-controlled polymorphism in the in vivo assembly of 180-subunit and 120-subunit virions from a single capsid protein
    • Krol M.A., Olson N.H., Tate J., Johnson J.E., Baker T.S., and Ahlquist P. RNA-controlled polymorphism in the in vivo assembly of 180-subunit and 120-subunit virions from a single capsid protein. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 13650-13655
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13650-13655
    • Krol, M.A.1    Olson, N.H.2    Tate, J.3    Johnson, J.E.4    Baker, T.S.5    Ahlquist, P.6
  • 16
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R.A., Moss D.S., and Thornton J.M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231 (1993) 1049-1067
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 17
    • 0036060096 scopus 로고    scopus 로고
    • A molecular switch in the capsid protein controls the particle polymorphism in an icosahedral virus
    • Lokesh G.L., Gowri T.D., Satheshkumar P.S., Murthy M.R.N., and Savithri H.S. A molecular switch in the capsid protein controls the particle polymorphism in an icosahedral virus. Virology 292 (2002) 211-223
    • (2002) Virology , vol.292 , pp. 211-223
    • Lokesh, G.L.1    Gowri, T.D.2    Satheshkumar, P.S.3    Murthy, M.R.N.4    Savithri, H.S.5
  • 20
    • 0021112807 scopus 로고
    • Structure of tomato busy stunt virus IV. The virus particle at 2.9 Å resolution
    • Olson A.J., Bricogne G., and Harrison S.C. Structure of tomato busy stunt virus IV. The virus particle at 2.9 Å resolution. J. Mol. Biol. 171 (1983) 61-93
    • (1983) J. Mol. Biol. , vol.171 , pp. 61-93
    • Olson, A.J.1    Bricogne, G.2    Harrison, S.C.3
  • 21
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowsky Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowsky, Z.1    Minor, W.2
  • 26
    • 4444242208 scopus 로고    scopus 로고
    • T = 1 capsid structures of Sesbania mosaic virus coat protein mutants: Determinants of T = 3 and T = 1 capsid assembly
    • Sangita V., Lokesh G.L., Satheshkumar P.S., Vijay C.S., Saravanan V., Savithri H.S., and Murthy M.R.N. T = 1 capsid structures of Sesbania mosaic virus coat protein mutants: Determinants of T = 3 and T = 1 capsid assembly. J. Mol. Biol. 342 (2004) 987-999
    • (2004) J. Mol. Biol. , vol.342 , pp. 987-999
    • Sangita, V.1    Lokesh, G.L.2    Satheshkumar, P.S.3    Vijay, C.S.4    Saravanan, V.5    Savithri, H.S.6    Murthy, M.R.N.7
  • 27
    • 25144474643 scopus 로고    scopus 로고
    • The role of arginine-rich motif and beta-annulus in the assembly and stability of Sesbania mosaic virus capsids
    • Satheshkumar P.S., Lokesh G.L., Murthy M.R.N., and Savithri H.S. The role of arginine-rich motif and beta-annulus in the assembly and stability of Sesbania mosaic virus capsids. J. Mol. Biol. 353 (2005) 447-458
    • (2005) J. Mol. Biol. , vol.353 , pp. 447-458
    • Satheshkumar, P.S.1    Lokesh, G.L.2    Murthy, M.R.N.3    Savithri, H.S.4
  • 28
    • 0023053991 scopus 로고
    • Structure and assembly of turnip crinkle virus. II. Mechanism of reassembly in vitro
    • Sorger P.K., Stockley P.G., and Harrison S.C. Structure and assembly of turnip crinkle virus. II. Mechanism of reassembly in vitro. J. Mol. Biol 191 (1986) 639-658
    • (1986) J. Mol. Biol , vol.191 , pp. 639-658
    • Sorger, P.K.1    Stockley, P.G.2    Harrison, S.C.3
  • 29
    • 0029643791 scopus 로고
    • Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy
    • Speir J.A., Munshi S., Wang G., Baker T.S., and Johnson J.E. Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy. Structure 3 (1995) 63-78
    • (1995) Structure , vol.3 , pp. 63-78
    • Speir, J.A.1    Munshi, S.2    Wang, G.3    Baker, T.S.4    Johnson, J.E.5
  • 30
    • 0033946762 scopus 로고    scopus 로고
    • Sobemoviruses
    • Tamm T., and Truve E. Sobemoviruses. J. Virol. 74 (2000) 6231-6241
    • (2000) J. Virol. , vol.74 , pp. 6231-6241
    • Tamm, T.1    Truve, E.2
  • 31
    • 0038002093 scopus 로고    scopus 로고
    • The three-dimensional structure of cocksfoot mottle virus at 2.7 Å resolution
    • Tars K., Zeltins A., and Liljas L. The three-dimensional structure of cocksfoot mottle virus at 2.7 Å resolution. Virology 310 (2003) 287-297
    • (2003) Virology , vol.310 , pp. 287-297
    • Tars, K.1    Zeltins, A.2    Liljas, L.3
  • 34
    • 0034715825 scopus 로고    scopus 로고
    • Mechanism of capsid assembly for an icosahedral plant virus
    • Zlotnick A., Aldrich R., Johnson J.M., Ceres P., and Young M.J. Mechanism of capsid assembly for an icosahedral plant virus. Virology 277 (2000) 450-456
    • (2000) Virology , vol.277 , pp. 450-456
    • Zlotnick, A.1    Aldrich, R.2    Johnson, J.M.3    Ceres, P.4    Young, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.