EMD-60230

Single-particle
2.64 Å
EMD-60230 Deposition: 20/05/2024
Map released: 07/08/2024
Last modified: 18/12/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-60230

capsid of Vivrio cholerae typing phage VP1

EMD-60230

Single-particle
2.64 Å
EMD-60230 Deposition: 20/05/2024
Map released: 07/08/2024
Last modified: 18/12/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Vibrio cholerae phage VP1
Sample: Vibrio cholerae phage VP1

Deposition Authors: Liu HR , Pang H
Three-dimensional structures of Vibrio cholerae typing podophage VP1 in two states.
Pang H , Fan F, Zheng J, Xiao H, Tan Z, Song J, Kan B, Liu H
(2024) Structure , 32 , 2364 - 2374.e2
PUBMED: 39471801
DOI: doi:10.1016/j.str.2024.10.005
ISSN: 0969-2126
ASTM: STRUE6
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.