Foldon-guided self-assembly of ultra-stable protein fibers

Protein Science

Volumn 17, Issue 9, 2008, Pages 1475-1485

  Bhardwaj, Anshul ^a   Walker Kopp, Nancy ^a   Wilkens, Stephan ^a   Cingolani, Gino ^a  

^a State University of New York Upstate Medical University: College of Medicine   (United States)

Author keywords

Bacteriophage P22; Nanoscale building block for the design of protein nanodevices; Phage T4 foldon; Spontaneous refolding; Tail needle gp26

Indexed keywords

FIBRITIN; GUANIDINE; PROTEIN; PROTEIN P22; UNCLASSIFIED DRUG;

ARTICLE; BACTERIOPHAGE; BACTERIOPHAGE T4; BIOPHYSICS; CHEMICAL MODIFICATION; CHIMERA; DENATURATION; HIGH TEMPERATURE; MOLECULAR BIOLOGY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS;

BACTERIOPHAGE P22; BACTERIOPHAGE T4; ESCHERICHIA COLI; GUANIDINE; MODELS, CHEMICAL; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN RENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; TEMPERATURE; THERMODYNAMICS; VIRAL PROTEINS; VIRAL TAIL PROTEINS;

EID: 50049086981     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.036111.108     Document Type: Article

References (20)

1. Andrews, D., Butler, J.S., Al-Bassam, J., Joss, L., Winn-Stapley, D.A., Casjens, S., and Cingolani, G. 2005. Bacteriophage P22 tail accessory factor GP26 is a long triple-stranded coiled coil. J. Biol. Chem. 280: 5929-5933.
2. Astier, Y., Bayley, H., and Howorka, S. 2005. Protein components for nanodevices. Curr. Opin. Chem. Biol. 9: 576-584.
3. Bhardwaj, A., Olia, A.S., Walker-Kopp, N., and Cingolani, G. 2007. Domain organization and polarity of tail needle GP26 in the portal vertex structure of bacteriophage P22. J. Mol. Biol. 371: 374-387.
4. Boudko, S.P., Londer, Y.Y., Letarov, A.V., Sernova, N.V., Engel, J., and Mesyanzhinov, V.V. 2002. Domain organization, folding and stability of bacteriophage T4 fibritin, a segmented coiled-coil protein. Eur. J. Biochem. 269: 833-841.
5. Conley, M.P. and Wood, W.B. 1975. Bacteriophage T4 whiskers: A rudimentary environment-sensing device. Proc. Natl. Acad. Sci. 72: 3701-3705.
6. Frank, S., Kammerer, R.A., Mechling, D., Schulthess, T., Landwehr, R., Bann, J., Guo, Y., Lustig, A., Bachinger, H.P., and Engel, J. 2001. Stabilization of short collagen-like triple helices by protein engineering. J. Mol. Biol. 308: 1081-1089.
7. Frank, S., Boudko, S., Mizuno, K., Schulthess, T., Engel, J., and Bachinger, H.P. 2003. Collagen triple helix formation can be nucleated at either end. J. Biol. Chem. 278: 7747-7750.
8. Guthe, S., Kapinos, L., Moglich, A., Meier, S., Grzesiek, S., and Kiefhaber, T. 2004. Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin. J. Mol. Biol. 337: 905-915.
9. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
10. Letarov, A.V., Londer, Y.Y., Boudko, S.P., and Mesyanzhinov, V.V. 1999. The carboxy-terminal domain initiates trimerization of bacteriophage T4 fibritin. Biochemistry (Mosc.) 64: 817-823.
11. Ludtke, S.J., Baldwin, P.R., and Chiu, W. 1999. EMAN: Semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128: 82-97.
12. Olia, A.S., Casjens, S., and Cingolani, G. 2007. Structure of phage P22 cell envelope-penetrating needle. Nat. Struct. Mol. Biol. 14: 1221-1226.
13. Papanikolopoulou, K., Forge, V., Goeltz, P., and Mitraki, A. 2004a. Formation of highly stable chimeric trimers by fusion of an adenovirus fiber shaft fragment with the foldon domain of bacteriophage t4 fibritin. J. Biol. Chem. 279: 8991-8998.
14. Papanikolopoulou, K., Teixeira, S., Belrhali, H., Forsyth, V.T., Mitraki, A., and van Raaij, M.J. 2004b. Adenovirus fibre shaft sequences fold into the native triple β-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif. J. Mol. Biol. 342: 219-227.
15. Sadreyev, R.I. and Grishin, N.V. 2006. Exploring dynamics of protein structure determination and homology-based prediction to estimate the number of superfamilies and folds. BMC Struct. Biol. 6: 6. doi: 10.1186/1472-6807-6-6.
16. Sissoeff, L., Mousli, M., England, P., and Tuffereau, C. 2005. Stable trimerization of recombinant rabies virus glycoprotein ectodomain is required for interaction with the p75NTR receptor. J. Gen. Virol. 86: 2543-2552.
17. Stetefeld, J., Frank, S., Jenny, M., Schulthess, T., Kammerer, R.A., Boudko, S., Landwehr, R., Okuyama, K., and Engel, J. 2003. Collagen stabilization at atomic level: Crystal structure of designed (GlyProPro)10foldon. Structure 11: 339-346.
18. Tao, Y., Strelkov, S.V., Mesyanzhinov, V.V., and Rossmann, M.G. 1997. Structure of bacteriophage T4 fibritin: A segmented coiled coil and the role of the C-terminal domain. Structure 5: 789-798.
19. van Heel, M., Harauz, G., Orlova, E.V., Schmidt, R., and Schatz, M. 1996. A new generation of the IMAGIC image processing system. J. Struct. Biol. 116: 17-24.
20. Yang, X., Lee, J., Mahony, E.M., Kwong, P.D., Wyatt, R., and Sodroski, J. 2002. Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin. J. Virol. 76: 4634-4642.