Bacteriophage φ29 scaffolding protein gp7 before and after prohead assembly

Nature Structural Biology

Volumn 10, Issue 7, 2003, Pages 572-576

  Morais, Marc C ^a   Kanamarul, Shuji ^a   Badasso, Mohammed O ^b   Koti, Jaya S ^b   Owen, Barbara A L ^c   McMurray, Cynthia T ^c   Anderson, Dwight L ^b   Rossmann, Michael G ^a  

^a PURDUE UNIVERSITY   (United States)

^b UNIVERSITY OF MINNESOTA   (United States)

^c MAYO CLINIC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; DNA BINDING PROTEIN; DOUBLE STRANDED DNA; LEUCINE ZIPPER PROTEIN; PROTEIN GP7; TRANSFER FACTOR GCN4; UNCLASSIFIED DRUG; VIRUS PROTEIN; DNA;

ARTICLE; BACTERIOPHAGE; CONTROLLED STUDY; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; ESCHERICHIA COLI; GEL ELECTROPHORESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN STRUCTURE; VIRUS ASSEMBLY; VIRUS CAPSID; X RAY ANALYSIS; BACILLUS PHAGE; CHEMISTRY; METABOLISM; PROTEIN CONFORMATION; ULTRASTRUCTURE; X RAY CRYSTALLOGRAPHY;

ALISMATACEAE; ESCHERICHIA COLI; UNIDENTIFIED BACTERIOPHAGE;

BACILLUS PHAGES; CRYOELECTRON MICROSCOPY; CRYSTALLOGRAPHY, X-RAY; DNA; PROTEIN CONFORMATION; VIRAL PROTEINS;

EID: 0038419606     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb939     Document Type: Article

References (25)

1. Anderson, D. & Reilly, B. Morphogenesis of bacteriophage φ29. In Bacillus subtilis and Other Gram-Positive Bacteria: Biochemistry, Physiology, and Molecular Genetics (ed. Sonenshein, A.L., Hoch, J.A. & Losick, R.) 859-867 (American Society for Microbiology, Washington, DC, 1993).
2. Tao, Y. et al. Assembly of a tailed bacterial virus and its genome release studied in three dimensions. Cell 95, 431-437 (1998).
3. Hagen, E.W., Reilly, B.E., Tosi, M.E. & Anderson, D.L. Analysis of gene function of bacteriophage φ29 of Bacillus subtilis: identification of cistrons essential for viral assembly. J. Virol. 19, 501-517 (1976).
4. Guo, P. et al. Regulation of the phage φ29 prohead shape and size by the portal vertex. Virology 183, 366-373 (1991).
5. Guo, P., Peterson, C. & Anderson, D. Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage φ29. J. Mol. Biol. 197, 229-236 (1987).
6. Bjornsti, M.A., Reilly, B.E. & Anderson, D.L. Morphogenesis of bacteriophage φ29 of Bacillus subtilis: oriented and quantized in vitro packaging of DNA-protein gp3. J. Virol. 45, 383-396 (1983).
7. Crick, F.H.C. The packing of α-helices: simple coiled-coils. Acta Crystallogr. 6, 689-697 (1953).
8. Branden, C. & Tooze, J. Introduction to Protein Structure (Garland Publishing, New York and London, 1991).
9. Lee, C.S. & Guo, P. Sequential interactions of structural proteins in phage φ29 procapsid assembly. J. Virol. 69, 5024-5032 (1995).
10. Fane, B.A. & Prevelige, P.E. Jr. Mechanism of scaffolding-assisted viral assembly. Adv. Prot. Chem. (in the press).
11. Sun, Y. et al. Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus. J. Mol. Biol. 297, 1195-1202 (2000).
12. Thuman-Commike, P.A. et al. Identification of additional coat-scaffolding interactions in a bacteriophage P22 mutant defective in maturation. J. Virol. 74, 3871-3873 (2000).
13. Jiang, W. et al. Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nat. Struct. Biol. 10, 131-135 (2003).
14. Peterson, C. et al. Composition and mass of the bacteriophage φ29 prohead and virion. J. Struct. Biol. 135, 18-25 (2001).
15. Parker, M.H., Brouillette, C.G. & Prevelige, P.E. Jr. Kinetic and calorimetric evidence for two distinct scaffolding protein binding populations within the bacteriophage P22 procapsid. Biochemistry 40, 8962-8970 (2001).
16. Aebi, U. et al. The transformation of τ particles into T4 heads. II. Transformations of the surface lattice and related observations on form determination. J. Supramol. Struct. 2, 253-275 (1974).
17. Ellenberger, T.E., Brandl, C.J., Struhl, K. & Harrison, S.C. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α-helices: crystal structure of the protein-DNA complex. Cell 71, 1223-1237 (1992).
18. Wichitwechkarn, J., Bailey, S., Bodley, J.W. & Anderson, D. Prohead RNA of bacteriophage φ29: size, stoichiometry and biological activity. Nucleic Acids Res. 17, 3459-3468 (1989).
19. Grimes, S. & Anderson, D. The bacteriophage φ29 packaging proteins supercoil the DNA ends. J. Mol. Biol. 266, 901-914 (1997).
20. Cowtan, K.D. & Main, P. Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints. Acta Crystallogr. D49, 148-157 (1993).
21. Cowtan, K.D. 'dm': an automated procedure for phase improvement by density modification. in Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography Vol. 31 (Daresbury Laboratory, Warrington, UK, 1994), 34-38.
22. Rossmann, M.G. The molecular replacement method. Acta Crystallogr. A 46, 73-82 (1990).
23. Navaza, J. AMoRe - an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
24. Brünger, A.T. et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
25. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).