Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions

Nature Structural Biology

Volumn 10, Issue 2, 2003, Pages 131-135

  Jiang, Wen ^a   Li, Zongli ^a   Zhang, Zhixian ^a   Baker, Matthew L ^a   Prevelige Jr , Peter E ^b   Chiu, Wah ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b University of Alabama at Birmingham   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; COAT PROTEIN; PROTEIN SUBUNIT;

ALPHA HELIX; ARTICLE; BACTERIOPHAGE P22; BETA SHEET; CONFORMATIONAL TRANSITION; CRYOELECTRON MICROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN PROCESSING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SALMONELLA TYPHIMURIUM;

BACTERIOPHAGE P22; CAPSID PROTEINS; CRYOELECTRON MICROSCOPY; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS;

BACTERIA (MICROORGANISMS); SALMONELLA TYPHIMURIUM; UNIDENTIFIED BACTERIOPHAGE;

EID: 0037313264     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb891     Document Type: Article

References (31)

1. King, J. & Chiu, W. The procapsid to capsid transition in double-stranded DNA bacteriophages, in Structural Biology of Viruses (eds. Chiu, W., Burnett, R.M. & Garcea, R.L.) 288-311 (Oxford Press, New York; 1997).
2. Prasad, B.V. et al. Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus. J. Mol. Biol. 231, 65-74 (1993).
3. Thuman-Commike, P.A. et al. Three-dimensional structure of scaffolding-containing phage P22 procapsids by electron cryo-microscopy. J. Mol. Biol. 260, 85-98 (1996).
4. Thuman-Commike, P.A. et al. Mechanism of scaffolding-directed virus assembly suggested by comparison of scaffolding-containing and scaffolding-lacking P22 procapsids. Biophys. J. 76, 3267-3277 (1999).
5. Zhang, Z. et al. Visualization of the maturation transition in bacteriophage P22 by electron cryomicroscopy. J. Mol. Biol. 297, 615-626 (2000).
6. Newcomb, W.W. et al. The ul6 gene product forms the portal for entry of DNA into the herpes simplex virus capsid. J. Virol. 75, 10923-10932 (2001).
7. Steven, A.C. & Spear, P.G. Herpesvirus capsid assembly and envelopment, in Strucutural Biology of Viruses (eds. Chiu, W., Burnett, R.M. & Garcea, R.L.) 312-351 (Oxford University Press, New York; 1997).
8. Galisteo, M.L. & King, J. Conformational transformations in the protein lattice of phage P22 procapsids. Biophys. J. 65, 227-235 (1993).
9. Jiang, W., Baker, M.L., Ludtke, S.J. & Chiu, W. Bridging the information gap: computational tools for intermediate resolution structure interpretation. J. Mol. Biol. 308, 1033-1044 (2001).
10. Wikoff, W.R. et al. Topologically linked protein rings in the bacteriophage HK97 capsid. Science 289, 2129-2133 (2000).
11. Kleywegt, G.J. & Jones, T.A. Detecting folding motifs and similarities in protein structures. Methods Enzymol. 277, 525-545 (1997).
12. Reinisch, K.M., Nibert, M.L. & Harrison, S.C. Structure ofthe reovirus core at 36 Å resolution. Nature 404, 960-967 (2000).
13. Zhou, Z.H. et al. Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus. Nat. Struct. Biol. 8, 868-873 (2001).
14. Grimes, J.M. et al. The atomic structure of the bluetongue virus core. Nature 395, 470-477 (1998).
15. Duda, R.L. Protein chainmail: catenated protein in viral capsids. Cell 94, 55-60 (1998).
16. Duda, R.L., Martincic, K. & Hendrix, R.W. Genetic basis of bacteriophage HK97 prohead assembly. J. Mol. Biol. 247, 636-647 (1995).
17. Conway, J.F., Duda, R.L., Cheng, N., Hendrix, R.W. & Steven, A.C. Proteolytic and conformational control of virus capsid maturation: the bacteriophage HK97 system. J. Mol. Biol. 253, 86-99 (1995).
18. Caspar, D. & Klug, A. Physical principles in the construction of regular viruses. Cold Spring Harb. Symp. Quant. Biol. 27, 1-24 (1962).
19. Aramli, L.A. & Teschke, C.M. Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein. J. Biol. Chem. 274, 22217-22224 (1999).
20. Prevelige, P.E. Jr., Thomas, D., Aubrey, K.L., Towse, S.A. & Thomas, G.J. Jr. Subunit conformational changes accompanying bacteriophage P22 capsid maturation. Biochemistry 32, 537-543 (1993).
21. Conway, J.F. et al. Virus maturation involving large subunit rotations and local refolding. Science 292, 744-748 (2001).
22. Prevelige, P.E. Jr., Thomas, D. & King, J. Scaffolding protein regulates the polymerization of P22 coat subunits into icosahedral shells in vitro. J. Mol. Biol. 202, 743-757 (1988).
23. Jiang, W. et al. Semi-automated icosahedral particle reconstruction at subnanometer resolution. J. Struct. Biol. 136, 214-225 (2001).
24. Saad, A., Zhou, Z.H., Jakana, J., Chiu, W. & Rixon, F.J. Roles of triplex and scaffolding proteins in herpes simplex virus type 1 capsid formation suggested by structures of recombinant particles. J. Virol. 73, 6821-6830 (1999).
25. Crowther, R.A. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 261, 221-230 (1971).
26. Ludtke, S.J., Baldwin, P.R. & Chiu, W. EMAN: semi-automated software for high resolution single particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
27. Zhou, Z.H. et al. Seeing the herpesvirus capsid at 8.5 A. Science 288, 877-880 (2000).
28. Harauz, G. & van Heel, M. Exact filters for general geometry three dimensional reconstruction. Optik 73, 146-156 (1986).
29. Carson, M. Ribbons. Methods Enzymol. 277,493-505 (1997).
30. Dougherty, M.T. & Chiu, W. Using animation to enhance 3D visualization: A strategy for a production and environment. Microsc. Microanal. 4 Suppl 2, 452-453 (1998).
31. He, J., Schmid, M.F., Zhou, Z.H., Rixon, F. & Chiu, W. Finding and using local symmetry in identifying lower domain movements in hexon subunits of the herpes simplex virus type 1 capsid. J. Mol. Biol. 309, 903-914 (2001).