THERMOSTABLE CHAPERONIN

这个子项目是许多利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 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。 Aacpn 10在七个亚基中的每一个上具有25个残基的延伸，其功能类似于GroES。Aacpn 10的C-末端尾部不负责蛋白质的超热稳定性。它仅用于减少高温下的聚集。尾部序列与任何已知的蛋白质结构域都不匹配，因此，二级结构是未知的。没有其他cpn 10蛋白质具有这样的C-末端尾，因此在组装的七聚体中的尾的位置是未知的。 测定GroEL-Aacpn 10-ADP复合物的冷冻电镜结构。将处理后的图像与GroEL-GroES-ADP复合物的已知cryo-EM和晶体结构进行比较。Aacpn 10在7个亚基中的每一个上具有25个残基的延伸。通过寻找实验复合物中存在的密度，而在已发表的复合物中不存在，确定此延伸的位置。

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.