Hermodson M A, Abad-Zapatero C, Abdel-Meguid S S, Pundak S, Rossmann M G, Tremaine J H
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907, USA.
Virology. 1982 May;119(1):133-49. doi: 10.1016/0042-6822(82)90071-x.
The amino acid sequence of the coat protein of southern bean mosaic virus has been determined. Chemical techniques were supplemented by a 2.8-A-resolution electron-density map which helped in assigning absolute positions for each peptide. Four amino acids and the placement of one heptapeptide near the amino terminus of the protein were interpolated by comparison with the partially known southern bean mosaic virus RNA sequence. The subunit is heavily lined with basic residues on the side facing the RNA. Subunit-subunit interactions are hydrophobic and ionic. The calcium site on the quasi-threefold axis has three glutamic residues as ligands. There is a disulfide bond, between Cys 168 and 176, within a sequence which is inserted in southern bean mosaic virus relative to the tomato bushy stunt virus structure. This portion is a helix nestling between the "beta-barrel" subunit structure and the RNA interior.
南方菜豆花叶病毒外壳蛋白的氨基酸序列已被确定。化学技术得到了分辨率为2.8埃的电子密度图的辅助，该图有助于确定每个肽段的绝对位置。通过与部分已知的南方菜豆花叶病毒RNA序列进行比较，插入了四个氨基酸以及一个七肽在该蛋白氨基末端附近的位置。亚基在面向RNA的一侧富含碱性残基。亚基-亚基相互作用是疏水的和离子性的。准三重轴上的钙位点有三个谷氨酸残基作为配体。在相对于番茄丛矮病毒结构插入南方菜豆花叶病毒的一个序列内，半胱氨酸168和176之间存在一个二硫键。这部分是一个螺旋，位于“β桶”亚基结构和RNA内部之间。
