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Protein folding and unfolding: proline cis - trans isomerization at the c subunits of F 1 F O -ATPase might open a high conductance ion channel
  • Salvatore Nesci
Salvatore Nesci
Universita degli Studi di Bologna

Corresponding Author:[email protected]

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The c subunits, which constitutes the c-ring apparatus of the F 1F O-ATPase, could be the main components of the mitochondrial permeability transition pore (mPTP). The well-known modulator of the mPTP formation and opening is the cyclophilin D (CyPD), a peptidyl-prolyl cis- trans isomerase. On the loop, which connects the two hairpin α-helix of c subunit, is present the unique proline residue (Pro 40) that could be a biological target of CyPD. Indeed, the proline cis- trans isomerization might provide the switch that interconverts the open/closed states of the pore by pulling out the c-ring lipid plug.
07 Jan 2022Submitted to PROTEINS: Structure, Function, and Bioinformatics
11 Jan 2022Submission Checks Completed
11 Jan 2022Assigned to Editor
12 Jan 2022Reviewer(s) Assigned
28 Apr 2022Review(s) Completed, Editorial Evaluation Pending
29 Apr 2022Editorial Decision: Revise Minor
04 May 20221st Revision Received
04 May 2022Submission Checks Completed
04 May 2022Assigned to Editor
04 May 2022Reviewer(s) Assigned
04 May 2022Review(s) Completed, Editorial Evaluation Pending
04 May 2022Editorial Decision: Accept
Nov 2022Published in Proteins: Structure, Function, and Bioinformatics volume 90 issue 11 on pages 2001-2005. 10.1002/prot.26383