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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of a mutant T=1 capsid of Sesbania mosaic virus: role of water molecules in capsid architecture and integrity
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Structure of a mutant T=1 capsid of Sesbania mosaic virus: role of water molecules in capsid architecture and integrity

机译：结构突变T = 1衣壳的田菁属衣壳花叶病毒:水分子的作用体系结构和完整性

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摘要

Deletion of the N-terminal 31 amino acids from the coat protein (CP) of Sesbania mosaic virus (SeMV) results in the formation of T=1 capsids. The X-ray crystal structure of CP-N Delta 31 mutant capsids reveals that the CP adopts a conformation similar to those of other T=1 mutants. The 40 N-terminal residues are disordered in CP-N Delta 31. The intersubunit hydrogen bonds closely resemble those of the native capsid. The role of water molecules in the SeMV structure has been analyzed for the first time using the present structure. As many as 139 of the 173 waters per subunit make direct contacts with the protein atoms. The water molecules form a robust scaffold around the capsid, stabilize the loops and provide integrity to the subunit. These waters constitute a network connecting diametrically opposite ends of the subunit. Such waters might act as nodes for conveying signals for assembly or disassembly across a large conformational space. Many water-mediated interactions are observed at various interfaces. The twofold interface, which has the smallest number of protein-protein contacts, is primarily held by water-mediated interactions. The present structure illuminates the role of water molecules in the structure and stability of the capsid and points out their possible significance in assembly.
机译：删除的氨基端31个氨基酸田菁花叶病毒外壳蛋白(CP) (SeMV)结果在T = 1衣壳的形成。x射线晶体结构CP-N三角洲31突变衣壳揭示了CP采用构象类似于其他T = 1突变体。氨基端残留在CP-N三角洲无序31. 像原生的衣壳。水分子在SeMV结构分析第一次使用结构。与蛋白质亚基直接联系原子。衣壳,稳定循环和为子单元提供完整性。构成一个网络连接完全子单元的两端。作为传递这样一个信号节点组装在大型的构象或拆卸空间。观察到在不同的接口。接口,它的最小数量蛋白质接触,主要是由water-mediated交互。水分子结构照明的作用衣壳和结构与稳定指出可能的意义组装。

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