title: Chaperoning through the mitochondrial intermembrane space.
abstract: The first high-resolution structure of a mitochondrial translocase complex, the Tim9-Tim10 chaperone, is reported by Webb et al. (2006) in a recent issue of Molecular Cell, providing important insight in the transport of hydrophobic proteins through the aqueous intermembrane space and the mechanisms of protein assembly.
authors.affiliation: Institut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Strasse 7, D-79104 Freiburg, Germany.
authors.forename: Nils
authors.initials: N
authors.lastname: Wiedemann
authors.forename: Nikolaus
authors.initials: N
authors.lastname: Pfanner
authors.forename: Agnieszka
authors.initials: A
authors.lastname: Chacinska
mesh_terms: D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D024101:Mitochondrial Proteins / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D046912:Multiprotein Complexes
chemical_list: D029968:Escherichia coli Proteins; D024101:Mitochondrial Proteins; D018832:Molecular Chaperones; D046912:Multiprotein Complexes; C478387:TIM10 protein, E coli; C478388:TIM9 protein, E coli