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http://purl.uniprot.org/citations/34315863http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34315863http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34315863http://www.w3.org/2000/01/rdf-schema#comment"How the human cytomegalovirus (HCMV) genome-the largest among human herpesviruses-is packaged, retained, and ejected remains unclear. We present the in situ structures of the symmetry-mismatched portal and the capsid vertex-specific components (CVSCs) of HCMV. The 5-fold symmetric 10-helix anchor-uncommon among known portals-contacts the portal-encircling DNA, which is presumed to squeeze the portal as the genome packaging proceeds. We surmise that the 10-helix anchor dampens this action to delay the portal reaching a "head-full" packaging state, thus facilitating the large genome to be packaged. The 6-fold symmetric turret, latched via a coiled coil to a helix from a major capsid protein, supports the portal to retain the packaged genome. CVSCs at the penton vertices-presumed to increase inner capsid pressure-display a low stoichiometry, which would aid genome retention. We also demonstrate that the portal and capsid undergo conformational changes to facilitate genome ejection after viral cell entry."xsd:string
http://purl.uniprot.org/citations/34315863http://purl.org/dc/terms/identifier"doi:10.1038/s41467-021-24820-3"xsd:string
http://purl.uniprot.org/citations/34315863http://purl.org/dc/terms/identifier"doi:10.1038/s41467-021-24820-3"xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/author"Dong L."xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/author"Dong L."xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/author"Li Z."xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/author"Li Z."xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/author"Yu X."xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/author"Yu X."xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/author"Pang J."xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/author"Pang J."xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/name"Nat. Commun."xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/pages"4538"xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/pages"4538"xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/title"Structural basis for genome packaging, retention, and ejection in human cytomegalovirus."xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/title"Structural basis for genome packaging, retention, and ejection in human cytomegalovirus."xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/34315863http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/34315863http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34315863
http://purl.uniprot.org/citations/34315863http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34315863