THERMOSTABLE CHAPERONIN

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目及 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 辅伴侣蛋白10（cpn 10;大肠杆菌中的GroES）是环状七聚体蛋白，当与cpn 60（大肠杆菌中的GroEL）复合时，其促进底物折叠。coli）。Cpn 10来自于超嗜热的古老细菌风产液菌（Aquifex aeolicus，Aacpn 10），它的每个单体的C-末端都有一个25个残基的延伸，这在其它Cpn 10蛋白中是没有的。早期的体外研究已经表明，七聚体作为载体或蛋白质功能并不需要这条尾巴。然而，在没有尾部的情况下，七聚体（Aacpn 10 del-25）容易聚集成纤维状堆叠环（Luke等人，2005年）。为了解释这一现象，Wittung-Stafshede小组用尾部的肽构建体进行了结合实验，以建立其对Aacpn 10 del-25的特异性，并提出使用冷冻电镜来确定其结构。

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 facili-tate substrate folding when in complex with cpn60 (GroEL in E. coli). Cpn10 from the hyper-thermophilic, an-cient 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 as-sembly 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.