Please use this identifier to cite or link to this item: 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
Appears in Collections:Staff Publications
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