5a79
From Proteopedia
Novel inter-subunit contacts in Barley Stripe Mosaic Virus revealed by cryo-EM
Structural highlights
FunctionCAPSD_BSMV Capsid protein self-assembles to form rod-shaped virions about 25 nm in diameter with a central canal enclosing the viral genomic RNA. Publication Abstract from PubMedBarley stripe mosaic virus (BSMV, genus Hordeivirus) is a rod-shaped single-stranded RNA virus similar to viruses of the structurally characterized and well-studied genus Tobamovirus. Here we report the first high-resolution structure of BSMV at 4.1 A obtained by cryo-electron microscopy. We discovered that BSMV forms two types of virion that differ in the number of coat protein (CP) subunits per turn and interactions between the CP subunits. While BSMV and tobacco mosaic virus CP subunits have a similar fold and interact with RNA using conserved residues, the axial contacts between the CP of these two viral groups are considerably different. BSMV CP subunits lack substantial axial contacts and are held together by a previously unobserved lateral contact formed at the virion surface via an interacting loop, which protrudes from the CP hydrophobic core to the adjacent CP subunit. These data provide an insight into diversity in structural organization of helical viruses. Novel Inter-Subunit Contacts in Barley Stripe Mosaic Virus Revealed by Cryo-Electron Microscopy.,Clare DK, Pechnikova EV, Skurat EV, Makarov VV, Sokolova OS, Solovyev AG, Orlova EV Structure. 2015 Aug 13. pii: S0969-2126(15)00287-7. doi:, 10.1016/j.str.2015.06.028. PMID:26278173[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|