AI Article Synopsis
- The PsbS protein in photosystem II helps plants protect themselves from light damage by responding to acidity changes in the thylakoid lumen.
- The study uses molecular dynamics simulations to explore how pH changes affect the structure and stability of the dimeric form of PsbS.
- Findings indicate that lower pH levels disrupt hydrogen bonds at the dimer interface, leading to a weaker protein interaction and promoting the protein's transition to a monomer, which is crucial for photoprotection.
Article Abstract
The photosystem II PsbS protein triggers the photoprotective mechanism of plants by sensing the acidification of the thylakoid lumen. Despite the mechanism of action of PsbS would require a pH-dependent monomerization of the dimeric form, a clear connection between the pH-induced structural changes and the dimer stability is missing. Here, by applying constant pH coarse-grained and all-atom molecular dynamics simulations, we investigate the pH-dependent structural response of the PsbS dimer. We find that the pH variation leads to structural changes in the lumen-exposed helices, located at the dimeric interface, providing an effective switch between PsbS and form. Moreover, the monomerization free energies reveal that in the neutral pH conformation, where the network of H-bond interactions at the dimeric interface is destroyed, the protein-protein interaction is weaker. Our results show how the pH-dependent conformations of PsbS affect their dimerization propensity, which is at the basis of the photoprotective mechanism.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9900633 | PMC |
| http://dx.doi.org/10.1021/acs.jpclett.2c03760 | DOI Listing |
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