EMD-7070

Single-particle
23.5 Å
EMD-7070 Deposition: 10/10/2017
Map released: 17/01/2018
Last modified: 25/12/2019
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-7070

Structure of the tail of the marine siphovirus TW1

EMD-7070

Single-particle
23.5 Å
EMD-7070 Deposition: 10/10/2017
Map released: 17/01/2018
Last modified: 25/12/2019
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Pseudoalteromonas phage TW1
Sample: Pseudoalteromonas phage TW1

Deposition Authors: Wang Z, Rossmann MG
Structure of the Marine Siphovirus TW1: Evolution of Capsid-Stabilizing Proteins and Tail Spikes.
Wang Z, Hardies SC, Fokine A, Klose T, Jiang W, Cho BC, Rossmann MG
(2018) Structure , 26 , 238 - 248.e3
PUBMED: 29290487
DOI: doi:10.1016/j.str.2017.12.001
ISSN: 1878-4186
ASTM: STRUE6
Abstract:
Marine bacteriophage TW1 belongs to the Siphoviridae family and infects Pseudoalteromonas phenolica. Mass spectrometry analysis has identified 16 different proteins in the TW1 virion. Functions of most of these proteins have been predicted by bioinformatic methods. A 3.6 Å resolution cryoelectron microscopy map of the icosahedrally averaged TW1 head showed the atomic structures of the major capsid protein, gp57, and the capsid-stabilizing protein, gp56. The gp57 structure is similar to that of the phage HK97 capsid protein. The gp56 protein has two domains, each having folds similar to that of the N-terminal part of phage λ gpD, indicating a common ancestry. The first gp56 domain clamps adjacent capsomers together, whereas the second domain is required for trimerization. A 6-fold-averaged reconstruction of the distal part of the tail showed that TW1 has six tail spikes, which are unusual for siphophages but are similar to the podophages P22 and Sf6, suggesting a common evolutionary origin of these spikes.