{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pena-Soler E"],"funding":["Instituto de Salud Carlos III","Seventh Framework Programme","Ministerio de Economía y Competitividad","Comunidad de Madrid (ES)"],"pagination":["e0186286"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5646864"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(10)"],"pubmed_abstract":["Sulfur trafficking in living organisms relies on transpersulfuration reactions consisting in the enzyme-catalyzed transfer of S atoms via activated persulfidic S across protein-protein interfaces. The recent elucidation of the mechanistic basis for transpersulfuration in the CsdA-CsdE model system has paved the way for a better understanding of its role under oxidative stress. Herein we present the crystal structure of the oxidized, inactivated CsdE dimer at 2.4 Å resolution. The structure sheds light into the activation of the Cys61 nucleophile on its way from a solvent-secluded position in free CsdE to a fully extended conformation in the persulfurated CsdA-CsdE complex. Molecular dynamics simulations of available CsdE structures allow to delineate the sequence of conformational changes "],"journal":["PloS one"],"pubmed_title":["Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE."],"pmcid":["PMC5646864"],"funding_grant_id":["BFU2010-22260-C02-02","BIO2009-11184","S2010/BD-2316","CTQ2015-66206-C2-2-R","PI12/01667","CTQ2015-66223-C2-2-P","ComplexINC (Contract No. 279039)","PET2008_0101"],"pubmed_authors":["Aranda J","Tunon I","Garces F","Vega MC","Fernandez FJ","Gomez S","Coll M","Pena-Soler E","Lopez-Estepa M"],"additional_accession":[]},"is_claimable":false,"name":"Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE.","description":"Sulfur trafficking in living organisms relies on transpersulfuration reactions consisting in the enzyme-catalyzed transfer of S atoms via activated persulfidic S across protein-protein interfaces. The recent elucidation of the mechanistic basis for transpersulfuration in the CsdA-CsdE model system has paved the way for a better understanding of its role under oxidative stress. Herein we present the crystal structure of the oxidized, inactivated CsdE dimer at 2.4 Å resolution. The structure sheds light into the activation of the Cys61 nucleophile on its way from a solvent-secluded position in free CsdE to a fully extended conformation in the persulfurated CsdA-CsdE complex. Molecular dynamics simulations of available CsdE structures allow to delineate the sequence of conformational changes ","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017","modification":"2026-04-18T17:04:54.376Z","creation":"2019-03-27T02:59:17Z"},"accession":"S-EPMC5646864","cross_references":{"pubmed":["29045454"],"doi":["10.1371/journal.pone.0186286"]}}