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Structural analysis of thermosome from hyperthermophilic archaeon Thermococcus
Suk Kyoung Kim1, Soon Rae Kim, Yun Hee Kim
1Division of Applied Life Science, Gyeongsang National University, Jinju, Korea.
Abstract:
The purification and characterization of thermostable chaperonin of the thermosome family from hyperthermophilic archaeon Thermococcus profunds are described. The purified thermosome is a homooligomeric complex and an ATPase with maximal activity at 80 degrees C. The electron micrographs obtained from negatively stained as well as frozen-hydrated specimen showed an eight-fold symmetry of chaperonin. They were about 15 nm height and 16 nm in diameter with a central cavity of 5 nm. In order to understand the ATPase cycling of thermosome, we analyzed the oligomeric structure of thermosome treated with several nucleotides.