Department of Molecular Physiology and Biological Physics, University of Virginia Charlottesville, VA, USA ; Midwest Center for Structural Genomics USA.
Evol Appl. 2013 Apr;6(3):434-49. doi: 10.1111/eva.12057. Epub 2013 Mar 13.
We present the crystal structures of two universal stress proteins (USP) from Archaeoglobus fulgidus and Nitrosomonas europaea in both apo- and ligand-bound forms. This work is the first complete synthesis of the structural properties of 26 USP available in the Protein Data Bank, over 75% of which were determined by structure genomics centers with no additional information provided. The results of bioinformatic analyses of all available USP structures and their sequence homologs revealed that these two new USP structures share overall structural similarity with structures of USPs previously determined. Clustering and cladogram analyses, however, show how they diverge from other members of the USP superfamily and show greater similarity to USPs from organisms inhabiting extreme environments. We compared them with other archaeal and bacterial USPs and discuss their similarities and differences in context of structure, sequential motifs, and potential function. We also attempted to group all analyzed USPs into families, so that assignment of the potential function to those with no experimental data available would be possible by extrapolation.
我们展示了来自古细菌（Archaeoglobus fulgidus）和硝化单胞菌（Nitrosomonas europaea）的两种普遍应激蛋白（USP）在 apo 和配体结合形式下的晶体结构。这项工作首次完整地综合了 26 种可在蛋白质数据库中获得的 USP 的结构特性，其中超过 75%是由结构基因组中心确定的，没有提供其他信息。对所有可用 USP 结构及其序列同源物的生物信息学分析结果表明，这两种新的 USP 结构与以前确定的 USP 结构具有总体结构相似性。然而，聚类和系统发育树分析表明，它们与 USP 超家族的其他成员有何不同，并且与生活在极端环境中的生物体中的 USP 更为相似。我们将它们与其他古细菌和细菌 USP 进行了比较，并根据结构、序列基序和潜在功能讨论了它们的相似性和差异。我们还尝试将所有分析的 USP 分组到家族中，以便通过推断将潜在功能分配给那些没有实验数据的 USP。
