5kip

Asymmetric unit for the coat proteins of phage Qbeta

spinqualitylabelsall models 5kip, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5kip is a 3 chain structure with sequence from Enterobacteria phage qbeta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [COAT_BPQBE] Forms the phage shell; binds to the phage RNA. Publication Abstract from PubMed Single-stranded (ss) RNA viruses infect all domains of life. To date, for most ssRNA virions, only the structures of the capsids and their associated protein components have been resolved to high resolution. Qbeta, an ssRNA phage specific for the conjugative F-pilus, has a T = 3 icosahedral lattice of coat proteins assembled around its 4,217 nucleotides of genomic RNA (gRNA). In the mature virion, the maturation protein, A2, binds to the gRNA and is required for adsorption to the F-pilus. Here, we report the cryo-electron microscopy (cryo-EM) structures of Qbeta with and without symmetry applied. The icosahedral structure, at 3.7-A resolution, resolves loops not previously seen in the published X-ray structure, whereas the asymmetric structure, at 7-A resolution, reveals A2 and the gRNA. A2 contains a bundle of alpha-helices and replaces one dimer of coat proteins at a twofold axis. The helix bundle binds gRNA, causing denser packing of RNA in its proximity, which asymmetrically expands the surrounding coat protein shell to potentially facilitate RNA release during infection. We observe a fixed pattern of gRNA organization among all viral particles, with the major and minor grooves of RNA helices clearly visible. A single layer of RNA directly contacts every copy of the coat protein, with one-third of the interactions occurring at operator-like RNA hairpins. These RNA-coat interactions stabilize the tertiary structure of gRNA within the virion, which could further provide a roadmap for capsid assembly. Asymmetric cryo-EM structure of the canonical Allolevivirus Qbeta reveals a single maturation protein and the genomic ssRNA in situ.,Gorzelnik KV, Cui Z, Reed CA, Jakana J, Young R, Zhang J Proc Natl Acad Sci U S A. 2016 Sep 26. pii: 201609482. PMID:27671640 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat protein

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