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.
Biophysical Structural Chemistry, Leiden Institute of Chemistry, P.O. Box 9502, 2300 RA Leiden, The Netherlands.
Anne-Marie M
AM
van Roon
Hugo H J
HH
Bink
Jasper R
JR
Plaisier
Cornelis W A
CW
Pleij
Jan Pieter
JP
Abrahams
Navraj S
NS
Pannu
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