THERMOSTABLE CHAPERONIN

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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.