Evolution of Bacteriophage Tails: Structure of T4 Gene Product 10

Journal of Molecular Biology

Volumn 358, Issue 3, 2006, Pages 912-921

  Leiman, Petr G ^a   Shneider, Mikhail M ^a,b   Mesyanzhinov, Vadim V ^b   Rossmann, Michael G ^a  

^a PURDUE UNIVERSITY   (United States)

^b SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

bacteriophage T4; baseplate; evolution; gp10; structural comparisons

Indexed keywords

GENE PRODUCT; GLYCOPROTEIN; GLYCOPROTEIN GP10; GLYCOPROTEIN GP11; GLYCOPROTEIN GP12; UNCLASSIFIED DRUG;

ARTICLE; BACTERIOPHAGE T4; CELL ADHESION; CONFORMATION; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; GENE DUPLICATION; MOLECULAR EVOLUTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STRUCTURE; RECEPTOR BINDING; STRUCTURAL GENOMICS; STRUCTURAL PROTEOMICS; STRUCTURE ANALYSIS; VIRAL GENETICS; VIRUS GENOME; VIRUS INFECTION;

EID: 33646029067     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.02.058     Document Type: Article

References (41)

1. Desplats C., and Krisch H.M. The diversity and evolution of the T4-type bacteriophages. Res. Microbiol. 154 (2003) 259-267
2. Wommack K.E., and Colwell R.R. Virioplankton: viruses in aquatic ecosystems. Microbiol. Mol. Biol. Rev. 64 (2000) 69-114
3. Ackermann H.W. Bacteriophage observations and evolution. Res. Microbiol. 154 (2003) 245-251
4. Hendrix R.W., Hatfull G.F., and Smith M.C.M. Bacteriophages with tails: chasing their origins and evolution. Res. Microbiol. 154 (2003) 253-257
5. Leiman P.G., Kanamaru S., Mesyanzhinov V.V., Arisaka F., and Rossmann M.G. Structure and morphogenesis of bacteriophage T4. Cell. Mol. Life Sci. 60 (2003) 2356-2370
6. Kostyuchenko V.A., Leiman P.G., Chipman P.R., Kanamaru S., van Raaij M.J., Arisaka F., et al. Three-dimensional structure of bacteriophage T4 baseplate. Nature Struct. Biol. 10 (2003) 688-693
7. Leiman P.G., Chipman P.R., Kostyuchenko V.A., Mesyanzhinov V.V., and Rossmann M.G. Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host. Cell 118 (2004) 419-429
8. Leiman P.G., Kostyuchenko V.A., Shneider M.M., Kurochkina L.P., Mesyanzhinov V.V., and Rossmann M.G. Structure of bacteriophage T4 gene product 11, the interface between the baseplate and short tail fibers. J. Mol. Biol. 301 (2000) 975-985
9. Thomassen E., Gielen G., Schütz M., Schoehn G., Abrahams J.P., Miller S., and van Raaij M.J. The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold. J. Mol. Biol. 331 (2003) 361-373
10. van Raaij M.J., Schoehn G., Burda M.R., and Miller S. Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre. J. Mol. Biol. 314 (2001) 1137-1146
11. Holm L., and Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
12. Bennett M.J., Schlunegger M.P., and Eisenberg D. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4 (1995) 2455-2468
13. Altschul S.F., Madden T.L., Schaffer A.A., Zhang J., Zhang Z., Miller W., and Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucl. Acids Res. 25 (1997) 3389-3402
14. Kostyuchenko V.A., Navruzbekov G.A., Kurochkina L.P., Strelkov S.V., Mesyanzhinov V.V., and Rossmann M.G. The structure of bacteriophage T4 gene product 9: the trigger for tail contraction. Structure 7 (1999) 1213-1222
15. Grundy F.J., and Howe M.M. Morphogenetic structures present in lysates of amber mutants of bacteriophage Mu. Virology 143 (1985) 485-504
16. Kondou Y., Kitazawa D., Takeda S., Tsuchiya Y., Yamashita E., Mizuguchi M., et al. Structure of the central hub of bacteriophage Mu baseplate determined by X-ray crystallography of gp44. J. Mol. Biol. 352 (2005) 976-985
17. Fokine A., Leiman P.G., Shneider M.M., Ahvaze B., Boeshans K.M., Steven A.C., et al. Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry. Proc. Natl Acad. Sci. USA 102 (2005) 7163-7168
18. Jiang W., Li Z., Zhang Z., Baker M.L., Prevelige Jr. P.E., and Chiu W. Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nature Struct. Biol. 10 (2003) 131-135
19. Morais M.C., Choi K.H., Koti J.S., Chipman P.R., Anderson D.L., and Rossmann M.G. Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudo atomic structure of φ{symbol}29. Mol. Cell 18 (2005) 149-159
20. Wikoff W.R., Liljas L., Duda R.L., Tsuruta H., Hendrix R.W., and Johnson J.E. Topologically linked protein rings in the bacteriophage HK97 capsid. Science 289 (2000) 2129-2133
21. Xiao C., Chipman P.R., Battisti A.J., Bowman V.D., Renesto P., Raoult D., and Rossmann M.G. Cryo-electron microscopy of the giant Mimivirus. J. Mol. Biol. 353 (2005) 493-496
22. Van Etten J.L., Lane L.C., and Meints R.H. Viruses and virus like particles of eukaryotic algae. Microbiol. Rev. 55 (1991) 586-620
23. Miller E., Kutter E., Mosig G., Arisaka F., Kunisawa T., and Rueger W. The bacteriophage T4 genome. Microbiol. Mol. Biol. Rev. 67 (2003) 86-156
24. Prilipov A.G., Selivanov N.A., Efimov V.P., Marusich E.I., and Mesyanzhinov V.V. Nucleotide sequences of bacteriophage T4 genes 9, 10 and 11. Nucl. Acids Res. 17 (1989) 3303
25. Leiman P.G., Shneider M.M., Kostyuchenko V.A., Chipman P.R., Mesyanzhinov V.V., and Rossmann M.G. Structure and location of gene product 8 in the bacteriophage T4 baseplate. J. Mol. Biol. 328 (2003) 821-833
26. Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
27. Hendrickson W.A., and Ogata C.M. Phase determination from multiwavelength anomalous diffraction measurements. Methods Enzymol. 276 (1997) 494-523
28. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
29. Terwilliger T.C., and Berendzen J. Automated MAD and MIR structure solution. Acta Crystallog. sect. D 55 (1999) 849-861
30. Terwilliger T.C. Automated structure solution, density modification and model building. Acta Crystallog. sect. D 58 (2002) 1937-1940
31. McRee D.E. XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
32. Sheldrick G.M. Macromolecular applications of SHELX. In: Rossmann M.G., and Arnold E. (Eds). Crystallography of Biological Macromolecules. International Tables for Crystallography vol. F (2001), Kluwer Academic Publishers, Dordrecht 734-738
33. Engh R.A., and Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A 47 (1991) 392-400
34. Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
35. Chacón P., and Wriggers W. Multi-resolution contour-based fitting of macromolecular structures. J. Mol. Biol. 317 (2002) 375-384
36. Rossmann M.G., Bernal R., and Pletnev S.V. Combining electron microscopic with X-ray crystallographic structures. J. Struct. Biol. 136 (2001) 190-200
37. Navaza J., Lepault J., Rey F.A., Álvarez-Rúa C., and Borge J. On the fitting of model electron densities into EM reconstructions: a reciprocal-space formulation. Acta Crystallog. sect. D 58 (2002) 1820-1825
38. Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24 (1991) 946-950
39. Merritt E.A., and Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277 (1997) 505-524
40. Sanner M.F., Olson A.J., and Spehner J.C. Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 38 (1996) 305-320
41. Chenna R., Sugawara H., Koike T., Lopez R., Gibson T.J., Higgins D.G., and Thompson J.D. Multiple sequence alignment with the Clustal series of programs. Nucl. Acids Res. 31 (2003) 3497-3500