The structure of tomato aspermy virus by X-ray crystallography

被引:26
作者
Lucas, RW [1 ]
Larson, SB [1 ]
Canady, MA [1 ]
McPherson, A [1 ]
机构
[1] Univ Calif Irvine, Dept Mol Biol & Biochem, Irvine, CA 92697 USA
基金
美国国家卫生研究院; 美国国家航空航天局;
关键词
Cucumovirus; diffraction; disulfide bridge; metal ions; nucleoprotein;
D O I
10.1016/S1047-8477(02)00561-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom data (effective resolution of 4 Angstrom ). 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 Angstrom diameter virion has the canonical "Swiss roll" beta-barrel topology with a distinctive amino-terminal a-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. (C) 2002 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:90 / 102
页数:13
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