6rrt
From Proteopedia
T=4 MS2 Virus-like-particle
Structural highlights
Function[CAPSD_BPMS2] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.[1] [2] [3] [4] [5] [6] Publication Abstract from PubMedBacteriophage MS2 is a positive-sense, single-stranded RNA virus encapsulated in an asymmetric T = 3 pseudo-icosahedral capsid. It infects Escherichia coli through the F-pilus, in which it binds through a maturation protein incorporated into its capsid. Cryogenic electron microscopy has previously shown that its genome is highly ordered within virions, and that it regulates the assembly process of the capsid. In this study, we have assembled recombinant MS2 capsids with non-genomic RNA containing the capsid incorporation sequence, and investigated the structures formed, revealing that T = 3, T = 4 and mixed capsids between these two triangulation numbers are generated, and resolving structures of T = 3 and T = 4 capsids to 4 A and 6 A respectively. We conclude that the basic MS2 capsid can form a mix of T = 3 and T = 4 structures, supporting a role for the ordered genome in favouring the formation of functional T = 3 virions. Bacteriophage MS2 displays unreported capsid variability assembling T = 4 and mixed capsids.,de Martin Garrido N, Crone MA, Ramlaul K, Simpson PA, Freemont PS, Aylett CHS Mol Microbiol. 2020 Jan;113(1):143-152. doi: 10.1111/mmi.14406. Epub 2019 Nov 5. PMID:31618483[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Bpms2 | Large Structures | Aylett, C H.S | Crone, M A | Freemont, P S | Garrido, N de Martin | Ramlaul, K | Simpson, P A | Bacteriophage | Ms2 | T=4 | Virus like particle | Vlp
