{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dieter EM"],"funding":["Basic Energy Sciences","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["2318-2333"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12375889"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["599(16)"],"pubmed_abstract":["Methanogenic archaea are particularly rich in iron-sulfur proteins, yet their roles remain largely enigmatic. Here, we characterized a Methanococcus voltae (Mvo) protein from the domain of unknown function (DUF) 2193 family, a group of proteins present primarily in archaea and characterized by a conserved cysteine-rich C-terminal motif. MvoDUF2193 was heterologously expressed and characterized by a range of spectroscopic and analytical methods. The results demonstrate that MvoDUF2193 binds a single [4Fe-4S] cluster per subunit and that cluster occupancy regulates the transition from an apo tetramer to a [4Fe-4S] monomeric form. We hypothesize that MvoDUF2193 serves a regulatory role in the cell, mediated by [Fe-S] cluster binding and changes in oligomeric state."],"journal":["FEBS letters"],"pubmed_title":["Archaeal protein containing domain of unknown function 2193 undergoes oligomeric reconfiguration upon iron-sulfur cluster binding."],"pmcid":["PMC12375889"],"funding_grant_id":["R01GM125924","DE-SC0020246","DE‐SC0020246"],"pubmed_authors":["Xiong J","Dieter EM","Bothner B","Tokmina-Lukaszewska M","Guo Y","Larson J","Broderick WE","Green J","Broderick JB"],"additional_accession":[]},"is_claimable":false,"name":"Archaeal protein containing domain of unknown function 2193 undergoes oligomeric reconfiguration upon iron-sulfur cluster binding.","description":"Methanogenic archaea are particularly rich in iron-sulfur proteins, yet their roles remain largely enigmatic. Here, we characterized a Methanococcus voltae (Mvo) protein from the domain of unknown function (DUF) 2193 family, a group of proteins present primarily in archaea and characterized by a conserved cysteine-rich C-terminal motif. MvoDUF2193 was heterologously expressed and characterized by a range of spectroscopic and analytical methods. The results demonstrate that MvoDUF2193 binds a single [4Fe-4S] cluster per subunit and that cluster occupancy regulates the transition from an apo tetramer to a [4Fe-4S] monomeric form. We hypothesize that MvoDUF2193 serves a regulatory role in the cell, mediated by [Fe-S] cluster binding and changes in oligomeric state.","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-05-08T10:53:33.605Z","creation":"2026-05-02T03:07:21.913Z"},"accession":"S-EPMC12375889","cross_references":{"pubmed":["40715996"],"doi":["10.1002/1873-3468.70120"]}}