title: Structural analysis of thermosome from hyperthermophilic archaeon Thermococcus.
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.
authors.affiliation: Division of Applied Life Science, Gyeongsang National University, Jinju, Korea.
authors.forename: Suk Kyoung
authors.initials: SK
authors.lastname: Kim
authors.forename: Soon Rae
authors.initials: SR
authors.lastname: Kim
authors.forename: Yun Hee
authors.initials: YH
authors.lastname: Kim
authors.forename: Pyeongsu
authors.initials: P
authors.lastname: Kwack
authors.forename: Daeyoung
authors.initials: D
authors.lastname: Son
authors.forename: Gang-Won
authors.initials: GW
authors.lastname: Cheong
mesh_terms: 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
chemical_list: D019843:Archaeal Proteins; D009711:Nucleotides; D018833:Chaperonins; D056405:Thermosomes