8OZH
In situ cryoEM structure of Prototype Foamy Virus Env trimer
Summary for 8OZH
Entry DOI | 10.2210/pdb8ozh/pdb |
Related | 8OZJ 8OZK 8OZL 8OZM 8OZN 8OZP 8OZQ |
EMDB information | 17309 17311 17312 17313 17314 17315 17316 17317 17318 17319 17320 17321 17322 |
Descriptor | Envelope glycoprotein, PHOSPHATIDYLETHANOLAMINE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total) |
Functional Keywords | membrane fusion, envelope glycoprotein, foamy virus, mper, transmembrane, membrane protein, viral protein |
Biological source | Eastern chimpanzee simian foamy virus |
Total number of polymer chains | 12 |
Total formula weight | 1389586.04 |
Authors | Calcraft, T.,Nans, A.,Rosenthal, P.B. (deposition date: 2023-05-09, release date: 2024-07-10, Last modification date: 2024-10-23) |
Primary citation | Calcraft, T.,Stanke-Scheffler, N.,Nans, A.,Lindemann, D.,Taylor, I.A.,Rosenthal, P.B. Integrated cryoEM structure of a spumaretrovirus reveals cross-kingdom evolutionary relationships and the molecular basis for assembly and virus entry. Cell, 187:4213-4230.e19, 2024 Cited by PubMed Abstract: Foamy viruses (FVs) are an ancient lineage of retroviruses, with an evolutionary history spanning over 450 million years. Vector systems based on Prototype Foamy Virus (PFV) are promising candidates for gene and oncolytic therapies. Structural studies of PFV contribute to the understanding of the mechanisms of FV replication, cell entry and infection, and retroviral evolution. Here we combine cryoEM and cryoET to determine high-resolution in situ structures of the PFV icosahedral capsid (CA) and envelope glycoprotein (Env), including its type III transmembrane anchor and membrane-proximal external region (MPER), and show how they are organized in an integrated structure of assembled PFV particles. The atomic models reveal an ancient retroviral capsid architecture and an unexpected relationship between Env and other class 1 fusion proteins of the Mononegavirales. Our results represent the de novo structure determination of an assembled retrovirus particle. PubMed: 39013471DOI: 10.1016/j.cell.2024.06.017 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.91 Å) |
Structure validation
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