5VKU
An atomic structure of the human cytomegalovirus (HCMV) capsid with its securing layer of pp150 tegument protein
This is a non-PDB format compatible entry.
Summary for 5VKU
| Entry DOI | 10.2210/pdb5vku/pdb |
| EMDB information | 8703 |
| Descriptor | Tegument protein pp150, Major capsid protein, Small capsomere-interacting protein, ... (5 entities in total) |
| Functional Keywords | icosahedral, capsid, tegument, herpesvirus, virus |
| Biological source | Human cytomegalovirus (strain AD169) (Human herpesvirus 5 strain AD169, HHV-5) More |
| Total number of polymer chains | 62 |
| Total formula weight | 3610917.40 |
| Authors | |
| Primary citation | Yu, X.,Jih, J.,Jiang, J.,Zhou, Z.H. Atomic structure of the human cytomegalovirus capsid with its securing tegument layer of pp150. Science, 356:-, 2017 Cited by PubMed Abstract: Herpesviruses possess a genome-pressurized capsid. The 235-kilobase genome of human cytomegalovirus (HCMV) is by far the largest of any herpesvirus, yet it has been unclear how its capsid, which is similar in size to those of other herpesviruses, is stabilized. Here we report a HCMV atomic structure consisting of the herpesvirus-conserved capsid proteins MCP, Tri1, Tri2, and SCP and the HCMV-specific tegument protein pp150-totaling ~4000 molecules and 62 different conformers. MCPs manifest as a complex of insertions around a bacteriophage HK97 gp5-like domain, which gives rise to three classes of capsid floor-defining interactions; triplexes, composed of two "embracing" Tri2 conformers and a "third-wheeling" Tri1, fasten the capsid floor. HCMV-specific strategies include using hexon channels to accommodate the genome and pp150 helix bundles to secure the capsid via cysteine tetrad-to-SCP interactions. Our structure should inform rational design of countermeasures against HCMV, other herpesviruses, and even HIV/AIDS. PubMed: 28663444DOI: 10.1126/science.aam6892 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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