8TEW
Human cytomegalovirus penton vertex, CVSC-bound configuration
This is a non-PDB format compatible entry.
Summary for 8TEW
| Entry DOI | 10.2210/pdb8tew/pdb |
| EMDB information | 41204 |
| Descriptor | Major capsid protein, Small capsomere-interacting protein, Large structural phosphoprotein, ... (8 entities in total) |
| Functional Keywords | tegument, penton, cvsc, intracellular transport, virus |
| Biological source | Human herpesvirus 5 strain AD169 More |
| Total number of polymer chains | 27 |
| Total formula weight | 2286346.19 |
| Authors | |
| Primary citation | Jih, J.,Liu, Y.T.,Liu, W.,Zhou, Z.H. The incredible bulk: Human cytomegalovirus tegument architectures uncovered by AI-empowered cryo-EM. Sci Adv, 10:eadj1640-eadj1640, 2024 Cited by PubMed Abstract: The compartmentalization of eukaryotic cells presents considerable challenges to the herpesvirus life cycle. The herpesvirus tegument, a bulky proteinaceous aggregate sandwiched between herpesviruses' capsid and envelope, is uniquely evolved to address these challenges, yet tegument structure and organization remain poorly characterized. We use deep-learning-enhanced cryogenic electron microscopy to investigate the tegument of human cytomegalovirus virions and noninfectious enveloped particles (NIEPs; a genome packaging-aborted state), revealing a portal-biased tegumentation scheme. We resolve atomic structures of portal vertex-associated tegument (PVAT) and identify multiple configurations of PVAT arising from layered reorganization of pUL77, pUL48 (large tegument protein), and pUL47 (inner tegument protein) assemblies. Analyses show that pUL77 seals the last-packaged viral genome end through electrostatic interactions, pUL77 and pUL48 harbor a head-linker-capsid-binding motif conducive to PVAT reconfiguration, and pUL47/48 dimers form 45-nm-long filaments extending from the portal vertex. These results provide a structural framework for understanding how herpesvirus tegument facilitates and evolves during processes spanning viral genome packaging to delivery. PubMed: 38394211DOI: 10.1126/sciadv.adj1640 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.02 Å) |
Structure validation
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