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Plant Polypeptide Hormone Systemin Prefers Polyproline II Conformation in Solution
Saikat Dutta Chowdhury1, Ansuman Lahiri1
1Department of Biophysics, Molecular Biology and Bioinformatics, University of Calcutta, 92, Acharya Prafulla Chandra Road, Kolkata 700009, West Bengal, India.
ACS Omega
|August 29, 2019
Summary
Systemin, a plant signaling peptide, shows a strong preference for polyproline II (PPII) conformations. Molecular dynamics simulations and docking support PPII structure
Area of Science:
- Biochemistry
- Structural Biology
- Computational Chemistry
Background:
- Systemin is the first discovered plant polypeptide hormone.
- Previous studies suggested a disordered structure in solution but a polyproline II (PPII) conformation via circular dichroism.
Purpose of the Study:
- To investigate the conformational preferences of systemin in solution.
- To explore the role of PPII conformations in systemin's bioactivity.
Main Methods:
- Molecular dynamics simulations using ff99SBildn and ff99IDPs force fields in explicit solvent.
- Analysis of predicted chemical shifts against NMR data.
- Docking calculations with the SR160 receptor.
Main Results:
- Both force fields indicated a high propensity for PPII-like conformations.
- Conformations matching NMR data showed increased PPII content, particularly with the ff99IDPs force field.
- Docking simulations also favored PPII structures.
Conclusions:
- Polyproline II (PPII) is a significant conformation for systemin.
- PPII structure may play a crucial role in systemin's biological activity.
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