title: Chaperonins: two rings for folding.
abstract: Chaperonins are ubiquitous chaperones found in Eubacteria, eukaryotic organelles (group I), Archaea and the eukaryotic cytosol (group II). They all share a common structure and a basic functional mechanism. Although a large amount of information has been gathered for the simpler group I, much less is known about group II chaperonins. Recent crystallographic and electron microscopy structures have provided new insights into the mechanism of these chaperonins and revealed important differences between group I and II chaperonins, mainly in the molecular rearrangements that take place during the functional cycle. These differences are evident for the most complex chaperonin, the eukaryotic cytosolic CCT, which highlights the uniqueness of this important molecular machine.
authors: Centro Nacional de Biotecnología (CNB-CSIC), Campus de la Universidad Autónoma de Madrid, Darwin 3, 28049 Madrid, Spain.
authors: Hugo
authors: H
authors: Yébenes
authors: Pablo
authors: P
authors: Mesa
authors: Inés G
authors: IG
authors: Muñoz
authors: Guillermo
authors: G
authors: Montoya
authors: José M
authors: JM
authors: Valpuesta
mesh_terms: D056404:Chaperonin Containing TCP-1 / Q000737:chemistry*; D056384:Group I Chaperonins / Q000737:chemistry*; D056385:Group II Chaperonins / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D056404:Chaperonin Containing TCP-1; D056384:Group I Chaperonins; D056385:Group II Chaperonins