Proteopedia

7lhd

The complete model of phage Qbeta virionThe complete model of phage Qbeta virion

Structural highlights

7lhd is a 182 chain structure with sequence from Escherichia virus Qbeta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 4.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MATA2_BPQBE Induces host cell lysis (PubMed:11892805). Inhibits host MurA activity thereby blocking the synthesis of murein precursors necessary for the host cell wall biosynthesis (PubMed:11423662). May be responsible for the attachment to the host pilus. Makes extensive contacts with the viral genome (PubMed:28111107).[1] [2] [3] [4]

Publication Abstract from PubMed

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 Qbeta, 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 T = 3 icosahedral, larger T = 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.

Structural Assembly of Qbeta Virion and Its Diverse Forms of Virus-like Particles.,Chang JY, Gorzelnik KV, Thongchol J, Zhang J Viruses. 2022 Jan 24;14(2). pii: v14020225. doi: 10.3390/v14020225. PMID:35215818[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Bernhardt TG, Wang IN, Struck DK, Young R. A protein antibiotic in the phage Qbeta virion: diversity in lysis targets. Science. 2001 Jun 22;292(5525):2326-9. PMID:11423662 doi:http://dx.doi.org/10.1126/science.1058289
  2. ↑ Karnik S, Billeter M. The lysis function of RNA bacteriophage Qbeta is mediated by the maturation (A2) protein. EMBO J. 1983;2(9):1521-6. PMID:11892805
  3. ↑ Reed CA, Langlais C, Wang IN, Young R. A(2) expression and assembly regulates lysis in Qbeta infections. Microbiology. 2013 Mar;159(Pt 3):507-14. doi: 10.1099/mic.0.064790-0. Epub 2013, Jan 17. PMID:23329676 doi:http://dx.doi.org/10.1099/mic.0.064790-0
  4. ↑ Rumnieks J, Tars K. Crystal Structure of the Maturation Protein from Bacteriophage Qbeta. J Mol Biol. 2017 Jan 19. pii: S0022-2836(17)30040-2. doi:, 10.1016/j.jmb.2017.01.012. PMID:28111107 doi:http://dx.doi.org/10.1016/j.jmb.2017.01.012
  5. ↑ Chang JY, Gorzelnik KV, Thongchol J, Zhang J. Structural Assembly of Qbeta Virion and Its Diverse Forms of Virus-like Particles. Viruses. 2022 Jan 24;14(2). pii: v14020225. doi: 10.3390/v14020225. PMID:35215818 doi:http://dx.doi.org/10.3390/v14020225

7lhd, resolution 4.60Å

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