PDF(Pubmed)
Abstract：
The Rib domain, which is often found as tandem-repeat structural modules in surface proteins of Gram-positive bacteria, plays important roles in mediating interactions of bacteria with their environments and hosts. A comprehensive structural analysis of various Rib domains is essential to fully understand their impact on the structure and functionality of these bacterial adhesins. To date, structural information has been limited for this expansive group of domains. In this study, the high-resolution crystal structure of the second member of the long Rib domain, a unique subclass within the Rib-domain family, derived from Limosilactobacillus reuteri is presented. The data not only demonstrate a highly conserved structure within the long Rib domain, but also highlight an evolutionary convergence in structural architecture with other modular domains found in cell-adhesion molecules.
摘要：
Rib域,通常在革兰氏阳性细菌的表面蛋白中发现串联重复结构模块，在介导细菌与其环境和宿主的相互作用中起着重要作用。各种Rib结构域的全面结构分析对于充分了解它们对这些细菌粘附素的结构和功能的影响至关重要。迄今为止,对于这一系列扩展的领域，结构信息是有限的。在这项研究中,长Rib域的第二成员的高分辨率晶体结构，Rib域家族中的唯一子类，提出了源自罗伊利硅藻杆菌的方法。数据不仅证明了长Rib域内的高度保守结构，但也强调了结构结构与细胞粘附分子中发现的其他模块化域的进化趋同。
