title: The ins and outs of a molecular chaperone machine.
abstract: Genetic and biochemical work has highlighted the biological importance of the GroEL/GroES (Hsp60/Hsp10; cpn60/cpn10) chaperone machine in protein folding. GroEL's donut-shaped structure has attracted the attention of structural biologists because of its elegance as well as the secrets (substrates) it can hide. The recent determination of the GroES and GroEL/GroES structures provides a glimpse of their plasticity, revealing dramatic conformational changes that point to an elaborate mechanism, coupling ATP hydrolysis to substrate release by GroEL.
authors.affiliation: Département de Biochimie Médicale, Université de Genève, Switzerland. Alexandra.Richardson@medicine.unige.ch
authors.forename: A
authors.initials: A
authors.lastname: Richardson
authors.forename: S J
authors.initials: SJ
authors.lastname: Landry
authors.forename: C
authors.initials: C
authors.lastname: Georgopoulos
mesh_terms: D017122:Bacteriophage T4 / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D018832:Molecular Chaperones