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A pH-Dependent Conformational Switch Controls N. meningitidis ClpP Protease Function.

Zev A Ripstein1,2, Siavash Vahidi1,2,3,4, John L Rubinstein1,2,5

  • 1Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.

Journal of the American Chemical Society
|November 24, 2020
PubMed
Summary
This summary is machine-generated.

A pH-dependent switch controls the shape of ClpP proteases, shifting between active extended and inactive compressed forms. This conformational change is crucial for regulating ClpP protease function in bacteria like Neisseria meningitidis.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • ClpP proteases are vital serine proteases involved in protein degradation.
  • They play critical roles in maintaining proteostasis in mitochondria and bacteria.
  • Targeting ClpP is a promising strategy for developing anti-cancer and anti-bacterial drugs.

Purpose of the Study:

  • To understand the structure-function relationships of ClpP proteases.
  • To investigate the conformational dynamics of ClpP from Neisseria meningitidis.
  • To identify the factors controlling different ClpP structural forms.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to visualize ClpP structures.
  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy was used to study ClpP dynamics.
  • Investigated the effect of pH on ClpP conformation.

Main Results:

  • Demonstrated a pH-dependent conformational switch in Neisseria meningitidis ClpP.
  • Identified an equilibrium between active extended and inactive compressed ClpP forms.
  • Showed that pH controls the population of these distinct conformational states.

Conclusions:

  • ClpP function is regulated by a pH-sensitive conformational switch.
  • This switch controls the equilibrium between active and inactive states.
  • Findings offer insights into ClpP's rugged energy landscape and conformational regulation.