Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the trigger factor chaperone.

ABSTRACT: Molecular chaperones often possess functional modules that are specialized in assisting the formation of specific structural elements, such as a disulfide bridges and peptidyl-prolyl bonds in cis form, in the client protein. A ribosome-associated molecular chaperone trigger factor (TF), which has a peptidyl-prolyl cis/trans isomerase (PPIase) domain, acts as a highly efficient catalyst in the folding process limited by peptidyl-prolyl isomerization. Herein we report a study on the mechanism through which TF recognizes the proline residue in the unfolded client protein during the cis/trans isomerization process. The solution structure of TF in complex with the client protein showed that TF recognizes the proline-aromatic motif located in the hydrophobic st

SUBMITTER: Kawagoe S 

PROVIDER: S-EPMC6166725 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature