Journal
STRUCTURE
Volume 22, Issue 2, Pages 281-290Publisher
CELL PRESS
DOI: 10.1016/j.str.2013.11.010
Keywords
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Funding
- Netherlands Organization for Scientific Research (NWO) [VENI 700.58.402]
- Deutsche Forschungsgemeinschaft
- Biotechnology and Biological Sciences Research Council [BBS/B/03955] Funding Source: researchfish
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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.
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