7ETO
C1 CVSC-binding penton vertex in the virion capsid of Human Cytomegalovirus
This is a non-PDB format compatible entry.
Summary for 7ETO
| Entry DOI | 10.2210/pdb7eto/pdb |
| EMDB information | 31301 |
| Descriptor | ORFL92C_UL32, Triplex capsid protein 2, Large tegument protein deneddylase, ... (8 entities in total) |
| Functional Keywords | c1 cvsc-binding penton vertex, virion capsid, viral protein |
| Biological source | Human cytomegalovirus (HHV-5, Human herpesvirus 5) More |
| Total number of polymer chains | 26 |
| Total formula weight | 2277850.26 |
| Authors | |
| Primary citation | Li, Z.,Pang, J.,Dong, L.,Yu, X. Structural basis for genome packaging, retention, and ejection in human cytomegalovirus. Nat Commun, 12:4538-4538, 2021 Cited by PubMed Abstract: 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. PubMed: 34315863DOI: 10.1038/s41467-021-24820-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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