biostudies-literatureMoffett ASstate of IllinoisNational Science Foundation2354-2363https://www.ebi.ac.uk/biostudies/studies/S-EPMC5768518biostudies-literatureUnknown113(11)Growing evidence supports the importance of protein S-glutathionylation as a regulatory post-translational modification with functional consequences for proteins. Discoveries of redox-state-dependent protein kinase S-glutathionylation have fueled discussion of redox-sensitive signaling. Following previously published experimental evidence for S-glutathionylation induced deactivation of the Arabidopsis thaliana kinase BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED RECEPTOR-LIKE KINASE 1 (BAK1), we investigated the consequences of S-glutathionylation on the equilibrium conformational ensemble of BAK1 using all-atom molecular dynamics simulations. We found that glutathionylation of C408 allosterically destabilizes the active-like state of BAK1 and stabilizes an inactive conformation known to recur Biophysical journalAllosteric Control of a Plant Receptor Kinase through S-Glutathionylation.PMC5768518OCI-0725070ACI-1238993Huber SCShukla DBender KWMoffett ASfalseAllosteric Control of a Plant Receptor Kinase through S-Glutathionylation.Growing evidence supports the importance of protein S-glutathionylation as a regulatory post-translational modification with functional consequences for proteins. Discoveries of redox-state-dependent protein kinase S-glutathionylation have fueled discussion of redox-sensitive signaling. Following previously published experimental evidence for S-glutathionylation induced deactivation of the Arabidopsis thaliana kinase BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED RECEPTOR-LIKE KINASE 1 (BAK1), we investigated the consequences of S-glutathionylation on the equilibrium conformational ensemble of BAK1 using all-atom molecular dynamics simulations. We found that glutathionylation of C408 allosterically destabilizes the active-like state of BAK1 and stabilizes an inactive conformation known to recur 2017-01-01T00:00:00Z2017 Dec2026-04-15T19:27:34.471Z2026-04-07T14:01:33.824ZS-EPMC57685182921198910.1016/j.bpj.2017.08.059