High-resolution insights into binding of unfolded polypeptides by the PPIase chaperone SlpA

• Main Authors: Löw, Christian, Nordlund, Pär, Quistgaard, Esben M.
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2013
• Subjects: DRNTU::Science::Biological sciences
• Online Access: https://hdl.handle.net/10356/100451; http://hdl.handle.net/10220/16249
• Institution: Nanyang Technological University

SlpA is a 2-domain protein consisting of an FK506-binding protein (FKBP) domain that harbors the peptidyl-prolyl cis/trans-isomerase (PPIase) active site and a small insert-in-flap (IF) domain that endows the protein with chaperone activity. We have determined the structure of SlpA from Escherichia...