6RRT

T=4 MS2 Virus-like-particle

Summary for 6RRT

• Entry DOI: 10.2210/pdb6rrt/pdb
• EMDB information: 4989 4990
• Descriptor: Capsid protein (1 entity in total)
• Functional Keywords: ms2, t=4, bacteriophage, vlp, virus like particle
• Biological source: Escherichia phage MS2
• Total number of polymer chains: 4
• Total formula weight: 55478.64

Authors

de Martin Garrido, N.,Ramlaul, K.,Simpson, P.A.,Crone, M.A.,Freemont, P.S.,Aylett, C.H.S. (deposition date: 2019-05-20, release date: 2020-07-08, Last modification date: 2024-05-22)

Primary citation

de Martin Garrido, N.,Crone, M.A.,Ramlaul, K.,Simpson, P.A.,Freemont, P.S.,Aylett, C.H.S.
Bacteriophage MS2 displays unreported capsid variability assembling T = 4 and mixed capsids.
Mol.Microbiol., 113:143-152, 2020

PubMed Abstract: Bacteriophage 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 Å and 6 Å 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.

PubMed: 31618483
DOI: 10.1111/mmi.14406

Experimental method

ELECTRON MICROSCOPY (6 Å)