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Volumn 17, Issue 10, 2008, Pages 1731-1739

Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particles

Author keywords

Coat protein; Dimer; Icosahedron; MS2; Octahedron; Virus

Indexed keywords

COAT PROTEIN; DIMER; MUTANT PROTEIN; PROTEIN SUBUNIT;

EID: 52949090437     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.036905.108     Document Type: Article
Times cited : (15)

References (28)
  • 2
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar, D.L.D. and Klug, A. 1962. Physical principles in the construction of regular viruses. Cold Spring Harb. Symp. Quant. Biol. 27: 1-24.
    • (1962) Cold Spring Harb. Symp. Quant. Biol , vol.27 , pp. 1-24
    • Caspar, D.L.D.1    Klug, A.2
  • 4
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4. 1994. The CCP4 Suite: Programs for protein crystallography. Acta Cryst. D50: 760-763.
    • Collaborative Computational Project, Number 4. 1994. The CCP4 Suite: Programs for protein crystallography. Acta Cryst. D50: 760-763.
  • 5
    • 36949077319 scopus 로고
    • Structure of small viruses
    • Crick, F.H.C. and Watson, J.D. 1956. Structure of small viruses. Nature 177: 473-475.
    • (1956) Nature , vol.177 , pp. 473-475
    • Crick, F.H.C.1    Watson, J.D.2
  • 7
    • 0027140498 scopus 로고
    • The refined structure of bacteriophage MS2 at 2.8 Å resolution
    • Golmohammadi, R., Valegärd, K., Fridborg, K., and Liljas, L. 1993. The refined structure of bacteriophage MS2 at 2.8 Å resolution. J. Mol. Biol. 234: 620-639.
    • (1993) J. Mol. Biol , vol.234 , pp. 620-639
    • Golmohammadi, R.1    Valegärd, K.2    Fridborg, K.3    Liljas, L.4
  • 9
    • 0034903751 scopus 로고    scopus 로고
    • Molray - a web interface between O and the POV-Ray ray tracer
    • Harris, M. and Jones, T.A. 2001. Molray - a web interface between O and the POV-Ray ray tracer. Acta Crystallogr. D Biol. Crystallogr. 57: 1201-1203.
    • (2001) Acta Crystallogr. D Biol. Crystallogr , vol.57 , pp. 1201-1203
    • Harris, M.1    Jones, T.A.2
  • 11
    • 0014674281 scopus 로고
    • The structure of viruses of the papillomapolyoma type V. tubular variants built of pentamers
    • Kiselev, N.A. and Klug, A. 1969. The structure of viruses of the papillomapolyoma type V. tubular variants built of pentamers. J. Mol. Biol. 40: 155-171.
    • (1969) J. Mol. Biol , vol.40 , pp. 155-171
    • Kiselev, N.A.1    Klug, A.2
  • 12
    • 0030589514 scopus 로고    scopus 로고
    • Phi/psi-chology: Ramachandran revisited
    • Kleywegt, G.J. and Jones, T.A. 1996. Phi/psi-chology: Ramachandran revisited. Structure 4: 1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 14
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. and Henrick, K. 2007. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372: 774-797.
    • (2007) J. Mol. Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 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. 1999. RNA-controlled polymorphism in the in vivo assembly of 180-subunit and 120-subunit virions from a single capsid protein. Proc. Natl. Acad. Sci. 96: 13650-13655.
    • (1999) Proc. Natl. Acad. Sci , 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
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B. and Richards, F.M. 1971. The interpretation of protein structures: Estimation of static accessibility. J. Mol. Biol. 55: 379-400.
    • (1971) J. Mol. Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 18
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • eds. C.W. Carter Jr. and R.M. Sweet, pp, Academic Press, New York
    • Otwinowski, Z. and Minor, W. 1996. Processing of X-ray diffraction data collected in oscillation mode. In Methods in enzymology (eds. C.W. Carter Jr. and R.M. Sweet), pp. 307-326. Academic Press, New York.
    • (1996) Methods in enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 19
    • 0031282522 scopus 로고    scopus 로고
    • Subunit fusion confers tolerance to peptide insertions in a virus coat protein
    • Peabody, D.S. 1997. Subunit fusion confers tolerance to peptide insertions in a virus coat protein. Arch. Biochem. Biophys. 347: 85-92.
    • (1997) Arch. Biochem. Biophys , vol.347 , pp. 85-92
    • Peabody, D.S.1
  • 20
    • 0029899266 scopus 로고    scopus 로고
    • Complementation of RNA binding site mutations in MS2 coat protein heterodimers
    • Peabody, D.S. and Lim, F. 1996. Complementation of RNA binding site mutations in MS2 coat protein heterodimers. Nucleic Acids Res. 24: 2352-2359.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2352-2359
    • Peabody, D.S.1    Lim, F.2
  • 21
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R.J. 2001. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. D Biol. Crystallogr. 57: 1373-1382.
    • (2001) Acta Crystallogr. D Biol. Crystallogr , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 22
    • 0024761528 scopus 로고
    • Polymorphism in the assembly of polyomavirus capsid protein VP1
    • Salunke, D.M., Caspar, D.L., and Garcea, R.L. 1989. Polymorphism in the assembly of polyomavirus capsid protein VP1. Biophys. J. 56: 887-900.
    • (1989) Biophys. J , vol.56 , pp. 887-900
    • Salunke, D.M.1    Caspar, D.L.2    Garcea, R.L.3
  • 23
    • 0004250834 scopus 로고    scopus 로고
    • 5th ed, pp, Lippincott, Philadelphia, PA
    • Seeger, C., Zoulim, F., and Mason, W.S. 2007. Fields virology, 5th ed., pp. 2977-3029 Lippincott, Philadelphia, PA.
    • (2007) Fields virology , pp. 2977-3029
    • Seeger, C.1    Zoulim, F.2    Mason, W.S.3
  • 24
    • 0030566047 scopus 로고    scopus 로고
    • Cosolute effect on crystallization of two dinucleotide complexes of bovine seminal ribonuclease from concentrated salt solutions
    • Sica, F., Adinolfi, S., Vitagliano, L., Zagari, A., Capasso, S., and Mazzarella, L. 1996. Cosolute effect on crystallization of two dinucleotide complexes of bovine seminal ribonuclease from concentrated salt solutions. J. Cryst. Growth 168: 192-197.
    • (1996) J. Cryst. Growth , vol.168 , pp. 192-197
    • Sica, F.1    Adinolfi, S.2    Vitagliano, L.3    Zagari, A.4    Capasso, S.5    Mazzarella, L.6
  • 25
    • 0031554914 scopus 로고    scopus 로고
    • The crystal structure of bacteriophage GA and a comparison of phages belonging to the major groups of Escherichia coli leviviruses
    • Tars, K., Bundule, M., Fridborg, K., and Liljas, L. 1997. The crystal structure of bacteriophage GA and a comparison of phages belonging to the major groups of Escherichia coli leviviruses. J. Mol. Biol. 271: 759-773.
    • (1997) J. Mol. Biol , vol.271 , pp. 759-773
    • Tars, K.1    Bundule, M.2    Fridborg, K.3    Liljas, L.4
  • 26
    • 0034608830 scopus 로고    scopus 로고
    • Crystal structure of phage PP7 from Pseudomonas aeruginosa at 3.7 Å resolution
    • Tars, K., Fridborg, K., Bundule, M., and Liljas, L. 2000. Crystal structure of phage PP7 from Pseudomonas aeruginosa at 3.7 Å resolution. Virology 272: 331-337.
    • (2000) Virology , vol.272 , pp. 331-337
    • Tars, K.1    Fridborg, K.2    Bundule, M.3    Liljas, L.4
  • 27
    • 0023053744 scopus 로고
    • Purification, crystallization and preliminary X-ray data of the bacteriophage MS2
    • Valegård, K., Unge, T., Montelius, I., Strandberg, B., and Fiers, W. 1986. Purification, crystallization and preliminary X-ray data of the bacteriophage MS2. J. Mol. Biol. 190: 587-591.
    • (1986) J. Mol. Biol , vol.190 , pp. 587-591
    • Valegård, K.1    Unge, T.2    Montelius, I.3    Strandberg, B.4    Fiers, W.5
  • 28
    • 0025344593 scopus 로고
    • The three-dimensional structure of the bacterial virus MS2
    • Valegård, K., Liljas, L., Fridborg, K., and Unge, T. 1990. The three-dimensional structure of the bacterial virus MS2. Nature 345: 36-41.
    • (1990) Nature , vol.345 , pp. 36-41
    • Valegård, K.1    Liljas, L.2    Fridborg, K.3    Unge, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.