8I4L

Capsid structure of the Cyanophage P-SCSP1u

Summary for 8I4L

• Entry DOI: 10.2210/pdb8i4l/pdb
• EMDB information: 35174
• Descriptor: The capsid protein(gp 19) of P-SCSP1u (1 entity in total)
• Functional Keywords: whole virus, capsid, cyanophage, t7-like virus, virus
• Biological source: Prochlorococcus phage P-SCSP1u
• Total number of polymer chains: 7
• Total formula weight: 246123.07

Authors

Liu, H.,Dang, S. (deposition date: 2023-01-19, release date: 2023-10-25, Last modification date: 2024-05-08)

Primary citation

Cai, L.,Liu, H.,Zhang, W.,Xiao, S.,Zeng, Q.,Dang, S.
Cryo-EM structure of cyanophage P-SCSP1u offers insights into DNA gating and evolution of T7-like viruses.
Nat Commun, 14:6438-6438, 2023

PubMed Abstract: Cyanophages, together with their host cyanobacteria, play important roles in marine biogeochemical cycles and control of marine food webs. The recently identified MPP-C (Marine Picocyanobacteria Podovirus clade C) cyanophages, belonging to the T7-like podoviruses, contain the smallest genomes among cyanopodoviruses and exhibit distinct infection kinetics. However, understanding of the MPP-C cyanophage infection process is hindered by the lack of high-resolution structural information. Here, we report the cryo-EM structure of the cyanophage P-SCSP1u, a representative member of the MPP-C phages, in its native form at near-atomic resolution, which reveals the assembly mechanism of the capsid and molecular interaction of the portal-tail complex. Structural comparison of the capsid proteins of P-SCSP1u and other podoviruses with known structures provides insights into the evolution of T7-like viruses. Furthermore, our study provides the near-atomic resolution structure of portal-tail complex for T7-like viruses. On the basis of previously reported structures of phage T7, we identify an additional valve and gate to explain the DNA gating mechanism for the T7-like viruses.

PubMed: 37833330
DOI: 10.1038/s41467-023-42258-7

Experimental method

ELECTRON MICROSCOPY (3.23 Å)