Structural analysis of thermosome from hyperthermophilic archaeon Thermococcus.
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.
Kim
Suk Kyoung
SK
Division of Applied Life Science, Gyeongsang National University, Jinju, Korea.
Kim
Soon Rae
SR
Kim
Yun Hee
YH
Kwack
Pyeongsu
P
Son
Daeyoung
D
Cheong
Gang-Won
GW
D019843:Archaeal Proteins / Q000737:chemistry*; D018833:Chaperonins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D009711:Nucleotides; D011485:Protein Binding; D019712:Thermococcus / Q000737:chemistry*; D056405:Thermosomes
D019843:Archaeal Proteins; D009711:Nucleotides; D018833:Chaperonins; D056405:Thermosomes