9LR9
Local reconstruction of bovine adenovirus type 3 capsid
This is a non-PDB format compatible entry.
Summary for 9LR9
| Entry DOI | 10.2210/pdb9lr9/pdb |
| EMDB information | 63322 |
| Descriptor | Hexon protein, PVI, Pre-histone-like nucleoprotein, ... (9 entities in total) |
| Functional Keywords | complex, viral protein |
| Biological source | Bovine adenovirus 3 More |
| Total number of polymer chains | 35 |
| Total formula weight | 1842707.25 |
| Authors | |
| Primary citation | Xiao, H.,Pang, H.,Zhou, J.,Feng, H.,Song, J.,Cheng, L.,Wang, L.,Liu, H. Structural Insights into Minor and Core Proteins of Bovine Adenovirus 3: Bridging Capsid and Genomic Core. J.Mol.Biol., 437:169208-169208, 2025 Cited by PubMed Abstract: Adenoviruses are double-stranded DNA viruses with broad relevance to human and animal health and considerable potential as therapeutic vectors. Despite extensive studies, the structural details of core and minor capsid proteins in adenoviruses remain poorly understood. In this study, the architecture of bovine adenovirus type 3 (BAdV-3), a member of the Mastadenovirus genus, was solved by cryo-electron microscopy. Our structure shows that BAdV-3 shares significant structural conservation with human adenoviruses. Atomic models were constructed for a previously uncharacterized region of the minor protein VI and for the core proteins V and Mu. The study revealed how core proteins bridge the genome and capsid, underscore the multifaceted roles of protein V in strengthening capsid stability and facilitating genome release. PubMed: 40381985DOI: 10.1016/j.jmb.2025.169208 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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