Capsid Structure of a Freshwater Cyanophage Siphoviridae Mic1.
capsid assembly
cement protein
cryo-EM structure
cyanophage
Journal
Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697
Informations de publication
Date de publication:
01 10 2019
01 10 2019
Historique:
received:
20
03
2019
revised:
11
06
2019
accepted:
12
07
2019
pubmed:
6
8
2019
medline:
21
5
2020
entrez:
6
8
2019
Statut:
ppublish
Résumé
Cyanobacteria are the most abundant photosynthetic microorganisms, the global distribution of which is mainly regulated by the corresponding cyanophages. A systematic screening of water samples in the Lake Chaohu enabled us to isolate a freshwater siphocyanophage that infects Microcystis wesenbergii, thus termed Mic1. Using cryoelectron microscopy, we solved the 3.5-Å structure of Mic1 capsid. The major capsid protein gp40 of an HK97-like fold forms two types of capsomers, hexons and pentons. The capsomers interact with each other via the interweaved N-terminal arms of gp40 in addition to a tail-in-mouth joint along the three-fold symmetric axis, resulting in the assembly of capsid in a mortise-and-tenon pattern. The novel-fold cement protein gp47 sticks at the two-fold symmetric axis and further fixes the capsid. These findings provide structural insights into the assembly of cyanophages, and set up a platform to explore the mechanism of specific interactions and co-evolution with cyanobacteria.
Identifiants
pubmed: 31378451
pii: S0969-2126(19)30235-7
doi: 10.1016/j.str.2019.07.003
pii:
doi:
Substances chimiques
Capsid Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1508-1516.e3Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.