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1
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0038392706
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Bacteriophage observations and evolution
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Classification of bacteriophages, according to their virion morphology, and comments on their host range and evolution. Approximately 96% of phages that have been examined with EM so far are tailed. The majority of the tailed phages (61%) belong to the Siphoviridae family. The Myoviridae and Podoviridae families constitute 25% and 14% of the tailed phages, respectively.
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Ackermann H.W. Bacteriophage observations and evolution. Res Microbiol. 154:2003;245-251 Classification of bacteriophages, according to their virion morphology, and comments on their host range and evolution. Approximately 96% of phages that have been examined with EM so far are tailed. The majority of the tailed phages (61%) belong to the Siphoviridae family. The Myoviridae and Podoviridae families constitute 25% and 14% of the tailed phages, respectively.
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Res Microbiol
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Ackermann, H.W.1
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Derosier, D.J.1
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0041819526
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Three-dimensional structure of bacteriophage T4 baseplate
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Cryo-EM reconstruction of the bacteriophage T4 tail tube-baseplate complex. Six baseplate protein structures, determined by X-ray crystallography, were fitted into the baseplate cryo-EM map. The baseplate was proposed to be stabilized by the short tail fibers, which run in a garland arrangement around the periphery of the baseplate.
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Kostyuchenko V.A., Leiman P.G., Chipman P.R., Kanamaru S., van Raaij M.J., Arisaka F., Mesyanzhinov V.V., Rossmann M.G. Three-dimensional structure of bacteriophage T4 baseplate. Nat Struct Biol. 10:2003;688-693 Cryo-EM reconstruction of the bacteriophage T4 tail tube-baseplate complex. Six baseplate protein structures, determined by X-ray crystallography, were fitted into the baseplate cryo-EM map. The baseplate was proposed to be stabilized by the short tail fibers, which run in a garland arrangement around the periphery of the baseplate.
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Nat Struct Biol
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Kostyuchenko, V.A.1
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Rossmann, M.G.8
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4
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0033570049
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The structure of bacteriophage T4 gene product 9: The trigger for tail contraction
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Kostyuchenko V.A., Navruzbekov G.A., Kurochkina L.P., Strelkov S.V., Mesyanzhinov V.V., Rossmann M.G. The structure of bacteriophage T4 gene product 9: the trigger for tail contraction. Structure Fold Des. 7:1999;1213-1222.
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Kostyuchenko, V.A.1
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Rossmann, M.G.6
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5
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0037203891
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Structure of the cell-puncturing device of bacteriophage T4
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The structure of the gp5-gp27 complex, comprising the baseplate hub, was determined by X-ray crystallography and fitted into a 17 Å resolution baseplate cryo-EM map. Gp5, or the tail lysozyme, is responsible for digesting the intermembrane peptidoglycan layer during infection. Its C-terminal triple-stranded β-helical domain was proposed to serve as the membrane-puncturing needle during tail contraction.
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Kanamaru S., Leiman P.G., Kostyuchenko V.A., Chipman P.R., Mesyanzhinov V.V., Arisaka F., Rossmann M.G. Structure of the cell-puncturing device of bacteriophage T4. Nature. 415:2002;553-557 The structure of the gp5-gp27 complex, comprising the baseplate hub, was determined by X-ray crystallography and fitted into a 17 Å resolution baseplate cryo-EM map. Gp5, or the tail lysozyme, is responsible for digesting the intermembrane peptidoglycan layer during infection. Its C-terminal triple-stranded β-helical domain was proposed to serve as the membrane-puncturing needle during tail contraction.
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Nature
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Kanamaru, S.1
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Arisaka, F.6
Rossmann, M.G.7
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6
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0034714138
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Structure of bacteriophage T4 gene product 11, the interface between the baseplate and short tail fibers
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Leiman P.G., Kostyuchenko V.A., Shneider M.M., Kurochkina L.P., Mesyanzhinov V.V., 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.
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Leiman, P.G.1
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7
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0242418196
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Structure and location of gene product 8 in the bacteriophage T4 baseplate
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The structure of gp8 was determined using X-ray crystallography and fitted into the cryo-EM reconstruction of the baseplate. Computer fitting procedures were used to establish the unique position of gp8 in the baseplate. The protein has been crystallized in two forms, one of which includes the conditions containing Br ions at 1 M concentration. The differences in the protein conformation between the two crystal forms were small and were proposed to be caused by the crystal lattice forces. Phasing, with the help of the ordered Br ions, was unsuccessful, probably as a result of the low redundancy and low resolution of the data.
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Leiman P.G., Shneider M.M., Kostyuchenko V.A., Chipman P.R., Mesyanzhinov V.V., Rossmann M.G. Structure and location of gene product 8 in the bacteriophage T4 baseplate. J Mol Biol. 328:2003;821-833 The structure of gp8 was determined using X-ray crystallography and fitted into the cryo-EM reconstruction of the baseplate. Computer fitting procedures were used to establish the unique position of gp8 in the baseplate. The protein has been crystallized in two forms, one of which includes the conditions containing Br ions at 1 M concentration. The differences in the protein conformation between the two crystal forms were small and were proposed to be caused by the crystal lattice forces. Phasing, with the help of the ordered Br ions, was unsuccessful, probably as a result of the low redundancy and low resolution of the data.
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Leiman, P.G.1
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Rossmann, M.G.6
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8
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0042463705
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The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold
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The crystal structure of the C-terminal fragment of gp12, the short tail fiber protein. During infection, the short tail fiber extends from the baseplate and binds to lipopolysaccharides on the cell outer surface. The receptor-binding interface of gp12 has been proposed.
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Thomassen E., Gielen G., Schutz M., Schoehn G., Abrahams J.P., Miller S., 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 The crystal structure of the C-terminal fragment of gp12, the short tail fiber protein. During infection, the short tail fiber extends from the baseplate and binds to lipopolysaccharides on the cell outer surface. The receptor-binding interface of gp12 has been proposed.
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Thomassen, E.1
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Coombs DH, Arisaka F: T4 tail structure and function. In Molecular Biology of Bacteriophage T4. Edited by Karam JD. Washington, DC: American Society for Microbiology; 1994:259-281.
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Ferguson P.L., Coombs D.H. Pulse-chase analysis of the in vivo assembly of the bacteriophage T4 tail. J Mol Biol. 297:2000;99-117.
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Kikuchi Y., King J. Genetic control of bacteriophage T4 baseplate morphogenesis. III. Formation of the central plug and overall assembly pathway. J Mol Biol. 99:1975;695-716.
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Kikuchi Y., King J. Genetic control of bacteriophage T4 baseplate morphogenesis. II. Mutants unable to form the central part of the baseplate. J Mol Biol. 99:1975;673-694.
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Kikuchi Y., King J. Genetic control of bacteriophage T4 baseplate morphogenesis. I. Sequential assembly of the major precursor, in vivo and in vitro. J Mol Biol. 99:1975;645-672.
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Arisaka F., Engel J., Klump H. Contraction and dissociation of the bacteriophage T4 tail sheath induced by heat and urea. Prog Clin Biol Res. 64:1981;365-379.
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Takeda S., Hoshida K., Arisaka F. Mapping of functional sites on the primary structure of the tail lysozyme of bacteriophage T4 by mutational analysis. Biochim Biophys Acta. 1384:1998;243-252.
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Kao S.H., McClain W.H. Roles of bacteriophage T4 gene 5 and gene s products in cell lysis. J Virol. 34:1980;104-107.
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Nakagawa H., Arisaka F., Ishii S. Isolation and characterization of the bacteriophage T4 tail-associated lysozyme. J Virol. 54:1985;460-466.
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Isolation of bacteriophage T4 baseplate proteins P7 and P8 and in vitro formation of the P10/P7/P8 assembly intermediate
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Plishker M.F., Rangwala S.H., Berget P.B. Isolation of bacteriophage T4 baseplate proteins P7 and P8 and in vitro formation of the P10/P7/P8 assembly intermediate. J Virol. 62:1988;400-406.
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King J. Bacteriophage T4 tail assembly: four steps in core formation. J Mol Biol. 58:1971;693-709.
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King, J.1
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P15 and P3, the tail completion proteins of bacteriophage T4, both form hexameric rings
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Zhao L., Kanamaru S., Chaidirek C., Arisaka F. P15 and P3, the tail completion proteins of bacteriophage T4, both form hexameric rings. J Bacteriol. 185:2003;1693-1700.
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Vianelli A., Wang G.R., Gingery M., Duda R.L., Eiserling F.A., Goldberg E.B. Bacteriophage T4 self-assembly: localization of gp3 and its role in determining tail length. J Bacteriol. 182:2000;680-688.
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Arisaka F., Tschopp J., Van Driel R., Engel J. Reassembly of the bacteriophage T4 tail from the core-baseplate and the monomeric sheath protein P18: a co-operative association process. J Mol Biol. 132:1979;369-386.
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King J. Assembly of the tail of bacteriophage T4. J Mol Biol. 32:1968;231-262.
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Watts N.R., Coombs D.H. Structure of the bacteriophage T4 baseplate as determined by chemical cross-linking. J Virol. 64:1990;143-154.
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Watts N.R., Hainfeld J., Coombs D.H. Localization of the proteins gp7, gp8 and gp10 in the bacteriophage T4 baseplate with colloidal gold:F(ab)2 and undecagold:Fab′ conjugates. J Mol Biol. 216:1990;315-325.
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The short tail-fiber of bacteriophage T4: Molecular structure and a mechanism for its conformational transition
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Makhov A.M., Trus B.L., Conway J.F., Simon M.N., Zurabishvili T.G., Mesyanzhinov V.V., Steven A.C. The short tail-fiber of bacteriophage T4: molecular structure and a mechanism for its conformational transition. Virology. 194:1993;117-127.
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Zhao L., Takeda S., Leiman P.G., Arisaka F. Stoichiometry and inter-subunit interaction of the wedge initiation complex, gp10-gp11, of bacteriophage T4. Biochim Biophys Acta. 1479:2000;286-292.
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Kanamaru S., Gassner N.C., Ye N., Takeda S., Arisaka F. The C-terminal fragment of the precursor tail lysozyme of bacteriophage T4 stays as a structural component of the baseplate after cleavage. J Bacteriol. 181:1999;2739-2744.
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Mosig G., Lin G.W., Franklin J., Fan W.H. Functional relationships and structural determinants of two bacteriophage T4 lysozymes: a soluble (gene e) and a baseplate-associated (gene 5) protein. New Biol. 1:1989;171-179.
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