7LHD

The complete model of phage Qbeta virion

This is a non-PDB format compatible entry.

Summary for 7LHD

• Entry DOI: 10.2210/pdb7lhd/pdb
• EMDB information: 23336
• Descriptor: Genomic RNA, Maturation protein A2, Capsid protein (3 entities in total)
• Functional Keywords: bacteriophage, virus, virion, virus-rna complex, virus/rna
• Biological source: Escherichia virus Qbeta; More
• Total number of polymer chains: 182
• Total formula weight: 3968882.48

Authors

Chang, J.Y.,Zhang, J. (deposition date: 2021-01-22, release date: 2022-01-26, Last modification date: 2024-11-20)

Primary citation

Chang, J.Y.,Gorzelnik, K.V.,Thongchol, J.,Zhang, J.
Structural Assembly of Q beta Virion and Its Diverse Forms of Virus-like Particles.
Viruses, 14:-, 2022

PubMed Abstract: The coat proteins (CPs) of single-stranded RNA bacteriophages (ssRNA phages) directly assemble around the genomic RNA (gRNA) to form a near-icosahedral capsid with a single maturation protein (Mat) that binds the gRNA and interacts with the retractile pilus during infection of the host. Understanding the assembly of ssRNA phages is essential for their use in biotechnology, such as RNA protection and delivery. Here, we present the complete gRNA model of the ssRNA phage Qβ, revealing that the 3' untranslated region binds to the Mat and the 4127 nucleotides fold domain-by-domain, and is connected through long-range RNA-RNA interactions, such as kissing loops. Thirty-three operator-like RNA stem-loops are located and primarily interact with the asymmetric A/B CP-dimers, suggesting a pathway for the assembly of the virions. Additionally, we have discovered various forms of the virus-like particles (VLPs), including the canonical = 3 icosahedral, larger = 4 icosahedral, prolate, oblate forms, and a small prolate form elongated along the 3-fold axis. These particles are all produced during a normal infection, as well as when overexpressing the CPs. When overexpressing the shorter RNA fragments encoding only the CPs, we observed an increased percentage of the smaller VLPs, which may be sufficient to encapsidate a shorter RNA.

PubMed: 35215818
DOI: 10.3390/v14020225

Experimental method

ELECTRON MICROSCOPY (4.6 Å)