7PE1
Cryo-EM structure of BMV-derived VLP expressed in E. coli and assembled in the presence of tRNA (tVLP)
This is a non-PDB format compatible entry.
Summary for 7PE1
| Entry DOI | 10.2210/pdb7pe1/pdb |
| EMDB information | 13344 |
| Descriptor | Coat protein (2 entities in total) |
| Functional Keywords | bmv, brome mosaic virus, capsid proteins, virus like particle |
| Biological source | Brome mosaic virus (BMV) |
| Total number of polymer chains | 180 |
| Total formula weight | 3702364.74 |
| Authors | Ruszkowski, M.,Strugala, A.,Indyka, P.,Urbanowicz, A. (deposition date: 2021-08-09, release date: 2022-03-02, Last modification date: 2024-07-17) |
| Primary citation | Ruszkowski, M.,Strugala, A.,Indyka, P.,Tresset, G.,Figlerowicz, M.,Urbanowicz, A. Cryo-EM reconstructions of BMV-derived virus-like particles reveal assembly defects in the icosahedral lattice structure. Nanoscale, 14:3224-3233, 2022 Cited by PubMed Abstract: The increasing interest in virus-like particles (VLPs) has been reflected by the growing number of studies on their assembly and application. However, the formation of complete VLPs is a complex phenomenon, making it difficult to rationally design VLPs with desired features . In this paper, we describe VLPs assembled from the recombinant capsid protein of brome mosaic virus (BMV). The analysis of VLPs was performed by Cryo-EM reconstructions and allowed us to visualize a few classes of VLPs, giving insight into the VLP self-assembly process. Apart from the mature icosahedral VLP practically identical with native virions, we describe putative VLP intermediates displaying non-icosahedral arrangements of capsomers, proposed to occur before the final disorder-order transition stage of icosahedral VLP assembly. Some of the described VLP classes show a lack of protein shell continuity, possibly resulting from too strong interaction with the cargo (in this case tRNA) with the capsid protein. We believe that our results are a useful prerequisite for the rational design of VLPs in the future and lead the way to the effective production of modified VLPs. PubMed: 35156989DOI: 10.1039/d1nr05650f PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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