THERMOSTABLE CHAPERONIN

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 共伴侣蛋白10(cpn10；在大肠杆菌中为groes)是环状七聚体蛋白，当与cpn60(在大肠杆菌中为groEL)形成复合体时，有助于底物折叠。Cpn10来自超高温、古老的细菌Aquifex aeolicus(Aacpn10)，它在每个单体中都有一个C端25个残基的延伸，这在任何其他cpn10蛋白中都没有发现。早期的体外研究表明，七聚体组装或蛋白质功能不需要这条尾巴。然而，如果没有尾巴，七聚体(Aacpn10del-25)很容易聚集成纤维状堆积环(Luke等人，2005年)。为了解释这一现象，Wittung-Stafshede团队进行了与尾部多肽结构的结合实验，以确定其对Aacpn10del-25的特异性，并建议使用冷冻EM来确定其结构。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Co-chaperonin proteins 10 (cpn10; GroES in Escherichia coli) are ring-shaped heptameric proteins that facilitate substrate folding when in complex with cpn60 (GroEL in E. coli). Cpn10 from the hyper-thermophilic, ancient bacterium, Aquifex aeolicus (Aacpn10) has a C-terminal 25-residue extension in each monomer not found in any other cpn10 protein. Earlier in vitro work has shown that this tail is not needed for heptamer assembly or protein function. Without the tail, however, the heptamers (Aacpn10del-25) readily aggregate into fibrillar stacked rings (Luke et al., 2005). To explain this phenomenon, Wittung-Stafshede group performed binding experiments with a peptide construct of the tail to establish its specificity for Aacpn10del-25 and proposed to use cryo-EM to determine its structure.