Trus B L, Roden R B, Greenstone H L, Vrhel M, Schiller J T, Booy F P
Computational Bioscience and Engineering Laboratory, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-5624, USA. B.L.T.
Nat Struct Biol. 1997 May;4(5):413-20. doi: 10.1038/nsb0597-413.
The three-dimensional structure of bovine papillomavirus has been determined to 9 A 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 A hole in the centre of hexavalent capsomeres is occluded in the pentavalent capsomeres. This raises the possibility that the L2 minor capsid protein is located in the centre of the pentavalent capsomeres. Inter-capsomere connections approximately 10 A in diameter were clearly resolved. These link adjacent capsomeres and are reminiscent of the helical connections that stabilize polyomavirus.
通过对淬冷冷冻病毒粒子的高分辨率、低剂量冷冻电子显微照片进行重建，已将牛乳头瘤病毒的三维结构解析到9埃的分辨率。尽管六价和五价壳粒形成主要衣壳蛋白L1的星形五聚体，但它们具有不同的高分辨率结构。最显著的是，六价壳粒中心的一个25埃的孔在五价壳粒中被封闭。这增加了次要衣壳蛋白L2位于五价壳粒中心的可能性。直径约10埃的壳粒间连接清晰可见。这些连接相邻的壳粒，让人联想到稳定多瘤病毒的螺旋连接。
