The role of disulfide bonds in a Solanum tuberosum saposin-like protein investigated using molecular dynamics.

ABSTRACT: The Solanum tuberosum plant specific insert (StPSI) has a defensive role in potato plants, with the requirements of acidic pH and anionic lipids. The StPSI contains a set of three highly conserved disulfide bonds that bridge the protein's helical domains. Removal of these bonds leads to enhanced membrane interactions. This work examined the effects of their sequential removal, both individually and in combination, using all-atom molecular dynamics to elucidate the role of disulfide linkages in maintaining overall protein tertiary structure. The tertiary structure was found to remain stable at both acidic (active) and neutral (inactive) pH despite the removal of disulfide linkages. The findings include how the dimer structure is stabilized and the impact on secondary structure on a residue-

SUBMITTER: Dupuis JH 

PROVIDER: S-EPMC7447066 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature