IMAGE-RECONSTRUCTION REVEALS THE COMPLEX MOLECULAR-ORGANIZATION OF ADENOVIRUS

被引：235

作者：

STEWART, PL ^{[1
]}

BURNETT, RM ^{[1
]}

CYRKLAFF, M ^{[1
]}

FULLER, SD ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB,BIOL STRUCT & BIOCOMP PROGRAMME,W-6900 HEIDELBERG,GERMANY

来源：

CELL | 1991年 / 67卷 / 01期

关键词：

D O I：

10.1016/0092-8674(91)90578-M

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 adenovirus has been determined by image reconstruction from cryoelectron micrographs. Comparison with the high resolution X-ray crystal structure of hexon, the major capsid protein, enabled an unusually detailed interpretation of the density map and confirmed the validity of the reconstruction. The hexon packing in the capsid shows more extensive intermolecular interfaces between facets than previously proposed. The reconstruction provides the first three-dimensional visualization of the vertex proteins, including the penton base and its associated protruding fiber. Three minor capsid proteins that stabilize and modulate capsomer interactions are revealed. One of these components stabilizes the group-of-nine hexons in the center of each facet and the other two bridge hexons in adjacent facets. The strategic positions of these proteins highlight the importance of cementing proteins in stabilizing a complex assembly.

引用

页码：145 / 154

页数：10

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