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

• المؤلفون الرئيسيون: Löw, Christian, Nordlund, Pär, Quistgaard, Esben M.
• مؤلفون آخرون: School of Biological Sciences
• التنسيق: مقال
• اللغة: English
• منشور في: 2013
• الموضوعات: DRNTU::Science::Biological sciences
• الوصول للمادة أونلاين: https://hdl.handle.net/10356/100451; http://hdl.handle.net/10220/16249
• المؤسسة: 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...