Summary information and primary citation
- PDB-id
-
1laj;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- virus-RNA
- Method
- X-ray (3.4 Å)
- Summary
- The structure of tomato aspermy virus by x-ray
crystallography
- Reference
-
Lucas RW, Larson SB, Canady MA, McPherson A (2002):
"The
Structure of Tomato Aspermy Virus by X-Ray
Crystallography." J.STRUCT.BIOL.,
139, 90-102. doi: 10.1016/S1047-8477(02)00561-0.
- Abstract
- The three-dimensional structure of tomato aspermy virus
(TAV) has been solved by X-ray crystallography and refined
to an R factor of 0.218 for 3.4-40 A data (effective
resolution of 4A). Molecular replacement, using cucumber
mosaic virus (Smith et al., 2000), provided phases for the
initial maps used for model building. The coat protein of
the 280 A diameter virion has the canonical "Swiss roll"
beta-barrel topology with a distinctive amino-terminal
alpha-helix directed into the interior of the virus where
it interacts with encapsidated RNA. The N-terminal helices
are joined to the beta-barrels of protein subunits by
extended polypeptides of six amino acids, which serve as
flexible hinges allowing movement of the helices in
response to local RNA distribution. Segments of three
nucleotides of partially disordered RNA interact with the
capsid, primarily through arginine residues, at interfaces
between A and B subunits. Side chains of cys64 and cys106
form the first disulfide observed in a cucumovirus,
including a unique cysteine, 106, in a region otherwise
conserved. A positive ion, putatively modeled as a
Mg(+)ion, lies on the quasi-threefold axis surrounded by
three quasi-symmetric glutamate 175 side chains.