全球对分子内同位素键的调查
Francesco Costa1, Ioannis Riziotis1, Antonina Andreeva1
1European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Hinxton, UK.
内分子异酸键增强了蛋白质的稳定性,并且在细菌和古生物的表面蛋白中广泛存在. 这项研究确定和结构性地描述了CLIPPER域,揭示了其广泛分布和功能重要性.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 微生物学 微生物学
背景情况:
- 蛋白质可以具有共价性分子内键,例如异类键,这增加了对各种攻击的稳定性.
- 在不同的生物体和蛋白质家族中,分子内异结的分布和结构多样性仍然在很大程度上没有特征.
研究的目的:
- 为了研究分子内同位素键在不同生物体中的蛋白质领域的流行和分布.
- 在结构和生物物理上表征含有分子内异酸键的新型蛋白质域,特别是CLIPPER域.
主要方法:
- 在AlphaFold数据库上的Isopeptor软件使用分子内异类键的大规模预测.
- 对已识别的蛋白质域进行了家族遗传分析.
- 进行X射线晶体学以了解决CLIPPER域的结构.
- 生物物理特征测定以评估热稳定性和对蛋白质分解的抗性.
主要成果:
- 内分子异酸键广泛分布在细菌和古生物的表面蛋白质中,特别是在纤维状粘附体和支柱中.
- 识别的债券仅限于Pfam家族的有限集中的两个不同的折叠 (CnaA类和CnaB类),包括10个新预测的家族.
- CLIPPER域 (DUF11) 广泛存在于细胞表面蛋白质中,当它含有内分子异酸键时,会赋予热稳定性和蛋白质分解性抵抗性.
结论:
- 微生物表面蛋白的内部分子异酸键是微生物表面蛋白的常见特征,对它们的稳定性有重大贡献.
- CLIPPER域是一个功能重要,在细菌和古生物中发现的进化保存域.
- 通过CLIPPER域的结构和生物物理特征,我们可以了解蛋白质通过分子内异酸键的稳定机制.
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