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https://doi.org/10.1107/S0907444906047330
Title: | From structure of the complex to understanding of the biology | Authors: | Rossmann, M.G Arisaka, F Battisti, A.J Bowman, V.D Chipman, P.R Fokine, A Hafenstein, S Kanamaru, S Kostyuchenko, V.A Mesyanzhinov, V.V Shneider, M.M Morais, M.C Leiman, P.G Palermo, L.M Parrish, C.R Xiao, C |
Keywords: | DNA bacteriophage binding site chemical structure chemistry conference paper conformation cryoelectron microscopy crystallization DNA packaging methodology protein conformation protein secondary structure ultrastructure virion virus virus assembly virus capsid X ray crystallography Bacteriophages Binding Sites Capsid Cryoelectron Microscopy Crystallization Crystallography, X-Ray DNA DNA Packaging Models, Molecular Molecular Conformation Protein Conformation Protein Structure, Secondary Virion Virus Assembly Viruses Canine parvovirus Parvovirus Rhinovirus |
Issue Date: | 2006 | Citation: | Rossmann, M.G, Arisaka, F, Battisti, A.J, Bowman, V.D, Chipman, P.R, Fokine, A, Hafenstein, S, Kanamaru, S, Kostyuchenko, V.A, Mesyanzhinov, V.V, Shneider, M.M, Morais, M.C, Leiman, P.G, Palermo, L.M, Parrish, C.R, Xiao, C (2006). From structure of the complex to understanding of the biology. Acta Crystallographica Section D: Biological Crystallography 63 (1) : 9-16. ScholarBank@NUS Repository. https://doi.org/10.1107/S0907444906047330 | Rights: | Attribution 4.0 International | Abstract: | The most extensive structural information on viruses relates to apparently icosahedral virions and is based on X-ray crystallography and on cryo-electron microscopy (cryo-EM) single-particle reconstructions. Both techniques lean heavily on imposing icosahedral symmetry, thereby obscuring any deviation from the assumed symmetry. However, tailed bacteriophages have icosahedral or prolate icosahedral heads that have one obvious unique vertex where the genome can enter for DNA packaging and exit when infecting a host cell. The presence of the tail allows cryo-EM reconstructions in which the special vertex is used to orient the head in a unique manner. Some very large dsDNA icosahedral viruses also develop special vertices thought to be required for infecting host cells. Similarly, preliminary cryo-EM data for the small ssDNA canine parvovirus complexed with receptor suggests that these viruses, previously considered to be accurately icosahedral, might have some asymmetric properties that generate one preferred receptor-binding site on the viral surface. Comparisons are made between rhinoviruses that bind receptor molecules uniformly to all 60 equivalent binding sites, canine parvovirus, which appears to have a preferred receptor-binding site, and bacteriophage T4, which gains major biological advantages on account of its unique vertex and tail organelle. © International Union of Crystallography 2007. | Source Title: | Acta Crystallographica Section D: Biological Crystallography | URI: | https://scholarbank.nus.edu.sg/handle/10635/181051 | ISSN: | 0907-4449 | DOI: | 10.1107/S0907444906047330 | Rights: | Attribution 4.0 International |
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