Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.

ABSTRACT: The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones. Multiple clamp-like binding sites hold the mitochondrial membrane proteins in a translocation-competent elongated form, thus mimicking characteristics of co-translational membrane insertion. The bound preprotein undergoes conformational dynamics within the chaperone binding clefts, pointing to a multitude of dynamic local bindin

SUBMITTER: Weinhaupl K 

PROVIDER: S-EPMC6242696 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature