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Substrate occupancy at the onset of oligomeric transitions of DegP

Thompson, Natalie J., Merdanovic, Melisa, Ehrmann, Michael, van Duijn, Esther and Heck, Albert J. R. 2014. Substrate occupancy at the onset of oligomeric transitions of DegP. Structure 22 (2) , pp. 281-290. 10.1016/j.str.2013.11.010

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The protease-chaperone DegP undergoes secondary through quaternary structural changes, regulating function and preventing indiscriminate proteolysis. Several structures of DegP oligomers have been observed, including the resting state 6-mer and the 12-mer and 24-mer active states. However, the precise events of the transition between the resting and active states still need to be elucidated. We used native mass spectrometry to demonstrate that binding of multiple substrate-mimicking peptide ligands to the DegP resting state occurs prior to the transition to an active conformation. This transition occurred at a 6-mer occupancy of 40% for each peptide ligand. We observed ligand-specific 9-mer formation with a maximum load of 9 peptides, whereas other substrates led to 12-mers accommodating 24 peptides. Based on these data, we present a model for the initial steps of substrate-induced transitions from the resting to active states of DegP.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: Q Science > QP Physiology
Additional Information: PDF uploaded in accordance with publisher's policies at (accessed 11.02.16). Available online 26 December 2013
Publisher: Elsevier
ISSN: 0969-2126
Date of First Compliant Deposit: 30 March 2016
Date of Acceptance: 20 November 2013
Last Modified: 30 Jun 2019 19:55

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