{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang H"],"funding":["Research Grants Council, University Grants Committee"],"pagination":["21379-21385"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12522045"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(45)"],"pubmed_abstract":["Metal ions may functionally inhibit metalloproteins <i>via</i> either replacement of intact metal cofactors or binding to allosteric sites <i>via</i> metalloallostery. Despite extensive studies, until now, it has not been fully understood how silver inhibits its authentic protein targets, particularly at the atomic level, largely owing to the lack of knowledge on the authentic protein targets of silver as well as the limited structures available. Herein we show that malate dehydrogenase (MDH) serves as a vital target of antimicrobial Ag<sup>+</sup> against <i>E. coli</i>. Ag<sup>+</sup> binds MDH at multiple sites and inhibits its activity <i>via</i> a non-competitive mechanism. Importantly, we successfully captured the Ag<sup>+</sup>-mediated \"open-to-closed\" conformational change of the "],"journal":["Chemical science"],"pubmed_title":["Unprecedented allosteric inhibition of &lt;i&gt;E. coli&lt;/i&gt; malate dehydrogenase by silver(i) from atomic resolution analysis."],"pmcid":["PMC12522045"],"funding_grant_id":["SRFS2122-7S04","17308921"],"pubmed_authors":["Wang M","Yang X","Li H","Hao Q","Yan A","Wang H","Sun H"],"additional_accession":[]},"is_claimable":false,"name":"Unprecedented allosteric inhibition of &lt;i&gt;E. coli&lt;/i&gt; malate dehydrogenase by silver(i) from atomic resolution analysis.","description":"Metal ions may functionally inhibit metalloproteins <i>via</i> either replacement of intact metal cofactors or binding to allosteric sites <i>via</i> metalloallostery. Despite extensive studies, until now, it has not been fully understood how silver inhibits its authentic protein targets, particularly at the atomic level, largely owing to the lack of knowledge on the authentic protein targets of silver as well as the limited structures available. Herein we show that malate dehydrogenase (MDH) serves as a vital target of antimicrobial Ag<sup>+</sup> against <i>E. coli</i>. Ag<sup>+</sup> binds MDH at multiple sites and inhibits its activity <i>via</i> a non-competitive mechanism. Importantly, we successfully captured the Ag<sup>+</sup>-mediated \"open-to-closed\" conformational change of the ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-06-05T18:34:06.662Z","creation":"2026-05-20T03:12:20.434Z"},"accession":"S-EPMC12522045","cross_references":{"pubmed":["41104151"],"doi":["10.1039/d5sc05183e"]}}