Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD

• Main Authors: Quistgaard, Esben M., Weininger, Ulrich, Ural-Blimke, Yonca, Modig, Kristofer, Nordlund, Pär, Akke, Mikael, Löw, Christian
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2016
• Subjects: Peptidyl-prolyl isomerase (PPIase); FK506-binding protein (FKBP)
• Online Access: https://hdl.handle.net/10356/84105; http://hdl.handle.net/10220/41603
• Institution: Nanyang Technological University

Background: Peptidyl-prolyl isomerases (PPIases) catalyze cis/trans isomerization of peptidyl-prolyl bonds, which is often rate-limiting for protein folding. SlyD is a two-domain enzyme containing both a PPIase FK506-binding protein (FKBP) domain and an insert-in-flap (IF) chaperone domain. To date,...