THERMOSTABLE CHAPERONIN

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。Aacpn10在7个亚基上都有25个残基延伸，其功能类似于GroES。Aacpn10的c端尾部与蛋白质的超热稳定性无关。它的作用只是在高温下减少聚集。尾序列不匹配任何已知的蛋白质结构域，因此，二级结构是未知的。没有其他cpn10蛋白具有这样的c末端尾巴，因此尾巴在组装的七聚体中的位置是未知的。确定GroEL-Aacpn10-ADP配合物的低温电镜结构。将处理后的图像与已知的cryo-EM和GroEL-GroES-ADP复合物的晶体结构进行比较。Aacpn10在7个亚基上各有25个残基延伸。通过寻找在实验综合体中存在的密度，而在已发表的综合体中不存在，确定该扩展的位置。

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. Aacpn10 has a 25-residue extension on each of the seven subunits which functions like GroES. C-terminal tail of Aacpn10 is not responsible for the protein's hyper-thermostability. It only functions to reduce aggregation at high temperatures. The tail sequence does not match any known protien domain, and as such, the secondary structure is unknown. No other cpn10 protein has such a C-terminal tail, so the location of the tail in the assembled heptamer is unknown. Determine cryo-EM structure of GroEL-Aacpn10-ADP complex. Compare the processed image to known cryo-EM and crystal structures of GroEL-GroES-ADP complex. Aacpn10 has a 25-residue extension on each of the seven subunits. By looking for density present in experimental complex that is not present in published complex, identify location of this extension.