8ZKK
Portal-tail of Vibrio cholerae typing phage mature VP1
Summary for 8ZKK
| Entry DOI | 10.2210/pdb8zkk/pdb |
| EMDB information | 60197 |
| Descriptor | nozzle gp16, portal gp5, adaptor gp12, ... (5 entities in total) |
| Functional Keywords | phage, virus, vibrio cholera phage, viral protein |
| Biological source | Vibrio cholerae More |
| Total number of polymer chains | 9 |
| Total formula weight | 309115.39 |
| Authors | |
| Primary citation | Pang, H.,Fan, F.,Zheng, J.,Xiao, H.,Tan, Z.,Song, J.,Kan, B.,Liu, H. Three-dimensional structures of Vibrio cholerae typing podophage VP1 in two states. Structure, 32:2364-2374.e2, 2024 Cited by PubMed Abstract: Lytic podophages (VP1-VP5) play crucial roles in subtyping Vibrio cholerae O1 biotype El Tor. However, until now no structures of these phages have been available, which hindered our understanding of the molecular mechanisms of infection and DNA release. Here, we determined the cryoelectron microscopy (cryo-EM) structures of mature and DNA-ejected VP1 structures at near-atomic and subnanometer resolutions, respectively. The VP1 head is composed of 415 copies of the major capsid protein gp7 and 11 turret-shaped spikes. The VP1 tail consists of an adapter, a nozzle, a slender ring, and a tail needle, and is flanked by three extended fibers I and six trimeric fibers II. Conformational changes of fiber II in DNA-ejected VP1 may cause the release of the tail needle and core proteins, forming an elongated tail channel. Our structures provide insights into the molecular mechanisms of infection and DNA release for podophages with a tail needle. PubMed: 39471801DOI: 10.1016/j.str.2024.10.005 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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