The C-terminal domains of adenovirus serotype 5 protein IX assemble into an antiparallel structure on the facets of the capsid.
Adenovirus serotype 5 protein IX (pIX) has two domains connected by a flexible linker. Three N-terminal domains form triskelions on the capsid facets that cement hexons together, and the C-terminal domains of four monomers form complexes toward the facet periphery. Here we present a cryoelectron microscopy structure of recombinant adenovirus with a peptide tag added to the C terminus of pIX. The structure, made up by several C termini of pIX, is longer at both ends than the wild-type protein, and Fabs directed against the tag bind to both ends of the oligomer, demonstrating that the pIX C termini associate in an antiparallel manner.
Fabry
Céline M S
CM
Université Joseph Fourier, Unit for Virus Host Cell Interaction, UMR 5233 UJF-EMBL-CNRS, Grenoble cedex 9, France.
Rosa-Calatrava
Manuel
M
Moriscot
Christine
C
Ruigrok
Rob W H
RW
Boulanger
Pierre
P
Schoehn
Guy
G
D000256:Adenoviridae / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure*; D000914:Antibodies, Viral / Q000378:metabolism; D036022:Capsid Proteins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure*; D020285:Cryoelectron Microscopy; D006801:Humans; D008958:Models, Molecular; D011485:Protein Binding; D020836:Protein Structure, Quaternary
D000914:Antibodies, Viral; D036022:Capsid Proteins; C018315:hexon capsid protein, Adenovirus