6J3Q

Capsid structure of a freshwater cyanophage Siphoviridae Mic1

Summary for 6J3Q

• Entry DOI: 10.2210/pdb6j3q/pdb
• EMDB information: 9774
• Descriptor: major capsid protein, cement protein (2 entities in total)
• Functional Keywords: cyanophage, siphoviridae, capsid, virus
• Biological source: Microcystis phage Mic1; More
• Total number of polymer chains: 26
• Total formula weight: 625020.41

Authors

Jin, H.,Jiang, Y.L.,Yang, F.,Zhang, J.T.,Li, W.F.,Zhou, K.,Ju, J.,Chen, Y.,Zhou, C.Z. (deposition date: 2019-01-05, release date: 2019-10-02, Last modification date: 2024-03-27)

Primary citation

Jin, H.,Jiang, Y.L.,Yang, F.,Zhang, J.T.,Li, W.F.,Zhou, K.,Ju, J.,Chen, Y.,Zhou, C.Z.
Capsid Structure of a Freshwater Cyanophage Siphoviridae Mic1.
Structure, 27:1508-, 2019

PubMed Abstract: 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.

PubMed: 31378451
DOI: 10.1016/j.str.2019.07.003

Experimental method

ELECTRON MICROSCOPY (3.53 Å)