Canady M A, Larson S B, Day J, McPherson A
Department of Biochemistry, University of California, Riverside 92521, USA.
Nat Struct Biol. 1996 Sep;3(9):771-81. doi: 10.1038/nsb0996-771.
The structure of turnip yellow mosaic virus (TYMV) has been solved to 3.2 A resolution and an R-value of 18.7%. The structure is consistent with models based on low resolution X-ray and electron microscopy studies, with pentameric and hexameric protein aggregates protruding from the surface and forming deep valleys at the quasi three-fold axes. The N-terminal 26 residues of the A-subunit are disordered, while those of the B- and C-subunits are seen to interact around the interior of the quasi six-fold cluster where they form an annulus. The three histidine residues of each protein subunit are located in the interior and accessible for interaction with the RNA genome. The appearance of the interior surface of the virus capsid, along with buried surface area calculations, suggest that a pentameric unit is lost during decapsidation.
芜菁黄花叶病毒（TYMV）的结构已解析至3.2埃分辨率，R值为18.7%。该结构与基于低分辨率X射线和电子显微镜研究的模型一致，五聚体和六聚体蛋白质聚集体从表面突出，并在准三重轴处形成深谷。A亚基的N端26个残基无序，而B亚基和C亚基的N端残基在准六重簇内部相互作用，形成一个环。每个蛋白质亚基的三个组氨酸残基位于内部，可与RNA基因组相互作用。病毒衣壳内表面的外观以及埋藏表面积计算表明，在脱壳过程中一个五聚体单元丢失。
