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首页> 外文期刊>Journal of Molecular Biology >Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes
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Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes

机译：结构和生化特征将口蹄疫病毒前导蛋白蛋白酶与其他木瓜样酶区分开

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摘要

The structures of the two leader protease (L-pro) variants of foot-and-mouth disease virus known to date were solved using crystals in which molecules were organized as molecular fibers. Such crystals diffract to a resolution of only approximately 3 Angstrom. This singular, pseudo-polymeric organization is present in a new L-pro crystal form showing a cubic packing. As molecular fiber formation appeared unrelated to crystallization conditions, we mutated the reactive cysteine 133 residue, which makes a disulfide bridge between adjacent monomers in the fibers, to serine. None of the intermolecular contacts found in the molecular fibers was present in crystals of this variant. Analysis of this L-pro structure, refined at 1.9 Angstrom resolution, enables a detailed definition of the active center of the enzyme, including the solvent organization. Assay of L-pro activity on a fluorescent hexapeptide substrate showed that L-pro, in contrast to papain, was highly sensitive to increases in the cation concentration and was active only across a narrow pH range. Examination of the L-pro structure revealed that three aspartate residues near the active site, not present in papain-like enzymes, are probably responsible for these properties. (C) 2000 Academic Press. [References: 36]
机译：迄今已知的口蹄疫病毒的两个前导蛋白酶（L-pro）变体的结构是使用晶体进行解析的，在该晶体中分子被组织为分子纤维。这样的晶体衍射到仅约3埃的分辨率。这种奇异的假聚合物结构以新的L-pro晶体形式存在，显示出立方堆积。由于分子纤维的形成似乎与结晶条件无关，我们突变了反应性半胱氨酸133残基，该残基在纤维中相邻单体之间形成了丝氨酸的二硫键。在该变体的晶体中没有分子纤维中发现的分子间接触。对这种L-pro结构的分析（以1.9埃的分辨率精制）可以详细定义酶的活性中心，包括溶剂的组织。荧光六肽底物上L-pro活性的测定表明，与木瓜蛋白酶相比，L-pro对阳离子浓度的增加高度敏感，并且仅在狭窄的pH范围内才有活性。对L-pro结构的研究表明，活性部位附近的三个天冬氨酸残基（不存在于木瓜蛋白酶样酶中）可能是这些特性的原因。 （C）2000学术出版社。 [参考：36]

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