CRYSTALLIZATION OF THE REOVIRUS TYPE-3 DEARING CORE CRYSTAL PACKING IS DETERMINED BY THE LAMBDA-2 PROTEIN

被引:48
作者
COOMBS, KM
FIELDS, BN
HARRISON, SC
机构
[1] HARVARD UNIV, DEPT BIOCHEM & MOLEC BIOL, CAMBRIDGE, MA 02138 USA
[2] HARVARD UNIV, SCH MED, DEPT MICROBIOL & MOLEC GENET, BOSTON, MA 02115 USA
[3] HARVARD UNIV, SCH MED, SHIPLEY INST MED, BOSTON, MA 02115 USA
[4] BRIGHAM & WOMENS HOSP, DEPT MED, BOSTON, MA 02115 USA
[5] HARVARD UNIV, HOWARD HUGHES MED INST, CAMBRIDGE, MA 02138 USA
关键词
D O I
10.1016/S0022-2836(05)80089-0
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
Core particles of reovirus type 3 Dearing (T3D) crystallized in the face-centered cubic space group F432 with dimensions of 1270 Å along each edge of the unit cell. Core particles of reovirus type 1 Lang (T1L) did not crystallize. Experiments with core particles derived from 27 different T1L × T3D reassortant viruses indicated that the L2 genome segment determined the capacity of cores to crystallize. This finding indicates important differences in the surface topography of the L2-translation product, the λ2 protein, of these two isolates, and suggests that important crystal contacts are mediated by this protein. These data are used to generate a model of the packing of reovirus core particles within the unit cell. © 1990 Academic Press Limited.
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页码:1 / 5
页数:5
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