Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 angstrom resolution

被引：149

作者：

Trus, BL

Roden, RBS

Greenstone, HL

Vrhel, M

Schiller, JT

Booy, FP

机构：

[1] NCI, CELLULAR ONCOL LAB, NIH, BETHESDA, MD 20892 USA

[2] NIAMSD, STRUCT BIOL LAB, NIH, BETHESDA, MD 20892 USA

[3] NIH, BIOMED ENGN & INSTRUMENTAT PROGRAM, NATL CTR RES RESOURCES, BETHESDA, MD 20892 USA

来源：

NATURE STRUCTURAL BIOLOGY | 1997年 / 4卷 / 05期

关键词：

D O I：

10.1038/nsb0597-413

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 bovine papillomavirus has been determined to 9 Angstrom resolution by reconstruction of high resolution, low dose cryo-electron micrographs of quench-frozen virions. Although hexavalent and pentavalent capsomeres form star-shaped pentamers of the major capsid protein L1, they have distinct high-resolution structures. Most prominently, a 25 Angstrom hole in the centre of hexavalent capsomeres is occluded in the pentavalent capsomeres. This raises the possibility that the 1.2 minor capsid protein is located in the centre of the pentavalent capsomeres. Intercapsomere connections similar to 10 Angstrom in diameter were clearly resolved. These link adjacent capsomeres and are reminiscent of the helical connections that stabilize polyomavirus.

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页码：413 / 420

页数：8

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