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。 Aacpn10在7个亚基中的每个亚基上都有一个25个残基的延伸，其功能类似于Groes。Aacpn10的C末端尾巴与蛋白质的超热稳定性无关。它只起到在高温下减少聚集的作用。尾部序列与任何已知的蛋白结构域都不匹配，因此二级结构未知。没有其他cpn10蛋白有这样的C-末端尾巴，所以在组装的七聚体中尾巴的位置是未知的。 确定了GroEL-Aacpn10-ADP络合物的低温电子显微镜结构。将处理后的图像与已知的GroEL-Groes-ADP络合物的低温电子显微镜和晶体结构进行比较。Aacpn10在7个亚基中的每一个上都有一个25个残基的延伸。通过寻找实验复合体中存在的密度，而不是已发表的复合体中存在的密度，确定这个延伸的位置。

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.