The N-terminal zinc binding domain of ClpX is a dimerization domain that modulates the chaperone function

• Main Authors: Wojtyra, U. A., Houry, Walid A., Thibault, Guillaume, Tuite, Ashleigh
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2013
• Subjects: DRNTU::Science::Biological sciences::Biochemistry
• Online Access: https://hdl.handle.net/10356/100398; http://hdl.handle.net/10220/17900
• Institution: Nanyang Technological University

Clp ATPases are unique chaperones that promote protein unfolding and subsequent degradation by proteases. The mechanism by which this occurs is poorly understood. Here we demonstrate that the N-terminal domain of ClpX is a C4-type zinc binding domain (ZBD) involved in substrate recognition. ZBD...