Crystal structure of an empty capsid of turnip yellow mosaic virus.
Empty capsids (artificial top component) of turnip yellow mosaic virus were co-crystallized with an encapsidation initiator RNA hairpin. No clear density was observed for the RNA, but there were clear differences in the conformation of a loop of the coat protein at the opening of the pentameric capsomer (formed by five A-subunits) protruding from the capsid, compared to the corresponding loop in the intact virus. Further differences were found at the N terminus of the A-subunit. These differences have implications for the mechanism of decapsidation of the virus, required for infection.
van Roon
Anne-Marie M
AM
Biophysical Structural Chemistry, Leiden Institute of Chemistry, P.O. Box 9502, 2300 RA Leiden, The Netherlands.
Bink
Hugo H J
HH
Plaisier
Jasper R
JR
Pleij
Cornelis W A
CW
Abrahams
Jan Pieter
JP
Pannu
Navraj S
NS
D002213:Capsid / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry; D012367:RNA, Viral / Q000737:chemistry; D017806:Tymovirus / Q000737:chemistry* / Q000235:genetics; D014764:Viral Proteins / Q000737:chemistry*
D021122:Protein Subunits; D012367:RNA, Viral; D014764:Viral Proteins