9JWB
Cyanophage A4 capsid asymmetric unit
Summary for 9JWB
| Entry DOI | 10.2210/pdb9jwb/pdb |
| EMDB information | 61850 |
| Descriptor | Major capsid protein, Plastocyanin-like domain-containing protein, Major cement (3 entities in total) |
| Functional Keywords | cyanophage, virus, capsid |
| Biological source | Anabaena phage A-4L More |
| Total number of polymer chains | 15 |
| Total formula weight | 353582.45 |
| Authors | Hou, P.,Li, Q.,Zhou, C.Z. (deposition date: 2024-10-10, release date: 2025-04-09, Last modification date: 2025-07-02) |
| Primary citation | Hou, P.,Zhou, R.Q.,Jiang, Y.L.,Yu, R.C.,Du, K.,Gan, N.,Ke, F.,Zhang, Q.Y.,Li, Q.,Zhou, C.Z. Cryo-EM structure of cyanopodophage A4 reveals a pentameric pre-ejectosome in the double-stabilized capsid. Proc.Natl.Acad.Sci.USA, 122:e2423403122-e2423403122, 2025 Cited by PubMed Abstract: Upon infection, the podophages usually eject a couple of proteins from the capsid to form a transmembrane ejectosome on the host cell membrane that facilitates the ejection of viral genome. However, it remains unclear how these proteins of pre-ejectosome are finely assembled at the center of highly packaged genome. Here, we report the intact structure of cyanopodophage A4, which consists of a capsid stabilized by two types of cement proteins and a short tail attached with six tail fibers. Notably, we find a pentameric pre-ejectosome at the core of capsid, which is composed of four ejection proteins wrapped into a coaxial cylinder of triple layers. Moreover, a segment of genomic DNA runs along the positively charged circular cleft formed by two ejection proteins. Based on the mortise-and-tenon architecture of pre-ejectosome in combination with previous studies, we propose a putative DNA packaging process and ejection mechanism for podophages. These findings largely enrich our knowledge on the assembly mechanism of podophages, which might facilitate the application of A4 as a chassis cyanophage in synthetic biology. PubMed: 40163721DOI: 10.1073/pnas.2423403122 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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