National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI094386
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
GM071940
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
DE025567
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
1S10RR23057
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
1S10OD018111
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
U24GM116792
United States
National Science Foundation (NSF, United States)
DBI-1338135
United States
National Science Foundation (NSF, United States)
DMR-1548924
United States
Citation
Journal: Nat Commun / Year: 2021 Title: Asymmetric reconstruction of mammalian reovirus reveals interactions among RNA, transcriptional factor µ2 and capsid proteins. Authors: Muchen Pan / Ana L Alvarez-Cabrera / Joon S Kang / Lihua Wang / Chunhai Fan / Z Hong Zhou / Abstract: Mammalian reovirus (MRV) is the prototypical member of genus Orthoreovirus of family Reoviridae. However, lacking high-resolution structures of its RNA polymerase cofactor μ2 and infectious ...Mammalian reovirus (MRV) is the prototypical member of genus Orthoreovirus of family Reoviridae. However, lacking high-resolution structures of its RNA polymerase cofactor μ2 and infectious particle, limits understanding of molecular interactions among proteins and RNA, and their contributions to virion assembly and RNA transcription. Here, we report the 3.3 Å-resolution asymmetric reconstruction of transcribing MRV and in situ atomic models of its capsid proteins, the asymmetrically attached RNA-dependent RNA polymerase (RdRp) λ3, and RdRp-bound nucleoside triphosphatase μ2 with a unique RNA-binding domain. We reveal molecular interactions among virion proteins and genomic and messenger RNA. Polymerase complexes in three Spinoreovirinae subfamily members are organized with different pseudo-D symmetries to engage their highly diversified genomes. The above interactions and those between symmetry-mismatched receptor-binding σ1 trimers and RNA-capping λ2 pentamers balance competing needs of capsid assembly, external protein removal, and allosteric triggering of endogenous RNA transcription, before, during and after infection, respectively.
History
Deposition
Apr 12, 2021
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Header (metadata) release
Jul 21, 2021
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Map release
Jul 21, 2021
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Update
Jul 21, 2021
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Current status
Jul 21, 2021
Processing site: PDBj / Status: Released
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Structure visualization
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Surface view with section colored by density value
In the structure databanks used in Yorodumi, some data are registered as the other names, "COVID-19 virus" and "2019-nCoV". Here are the details of the virus and the list of structure data.
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