3J0G
Homology model of E3 protein of Venezuelan Equine Encephalitis Virus TC-83 strain fitted with a cryo-EM map
Summary for 3J0G
| Entry DOI | 10.2210/pdb3j0g/pdb |
| Related | 3J0C |
| EMDB information | 5275 5276 |
| Descriptor | E3 protein (1 entity in total) |
| Functional Keywords | alphavirus, bioweapon, veev, virus |
| Biological source | Venezuelan equine encephalitis virus (VEEV) |
| Total number of polymer chains | 4 |
| Total formula weight | 25954.40 |
| Authors | Zhang, R.,Hryc, C.F.,Chiu, W. (deposition date: 2011-07-21, release date: 2011-08-24, Last modification date: 2024-11-27) |
| Primary citation | Zhang, R.,Hryc, C.F.,Cong, Y.,Liu, X.,Jakana, J.,Gorchakov, R.,Baker, M.L.,Weaver, S.C.,Chiu, W. 4.4 angstrom cryo-EM structure of an enveloped alphavirus Venezuelan equine encephalitis virus. Embo J., 30:3854-3863, 2011 Cited by PubMed Abstract: Venezuelan equine encephalitis virus (VEEV), a member of the membrane-containing Alphavirus genus, is a human and equine pathogen, and has been developed as a biological weapon. Using electron cryo-microscopy (cryo-EM), we determined the structure of an attenuated vaccine strain, TC-83, of VEEV to 4.4 Å resolution. Our density map clearly resolves regions (including E1, E2 transmembrane helices and cytoplasmic tails) that were missing in the crystal structures of domains of alphavirus subunits. These new features are implicated in the fusion, assembly and budding processes of alphaviruses. Furthermore, our map reveals the unexpected E3 protein, which is cleaved and generally thought to be absent in the mature VEEV. Our structural results suggest a mechanism for the initial stage of nucleocapsid core formation, and shed light on the virulence attenuation, host recognition and neutralizing activities of VEEV and other alphavirus pathogens. PubMed: 21829169DOI: 10.1038/emboj.2011.261 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.8 Å) |
Structure validation
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