{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jeyachandran VR"],"funding":["Howard Hughes Medical Institute","National Institutes of Health","NIGMS NIH HHS","National Science Foundation"],"pagination":["102153"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10197145"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["68"],"pubmed_abstract":["Radical S-adenosylmethionine (SAM) enzymes use a common catalytic core for diverse transformations. While all radical SAM enzymes bind a Fe<sub>4</sub>S<sub>4</sub> cluster via a characteristic tri-cysteine motif, many bind additional metal cofactors. Recently reported structures of radical SAM enzymes that use methylcobalamin or additional iron-sulfur clusters as cosubstrates show that these auxiliary units are anchored by N- and C-terminal domains that vary significantly in size and topology. Despite this architectural diversity, all use a common surface for auxiliary cofactor docking. In the sulfur insertion and metallocofactor assembly systems evaluated here, interaction with iron-sulfur cluster assembly proteins or downstream scaffold proteins is an important component of catalysis. S"],"journal":["Current opinion in chemical biology"],"pubmed_title":["Structural insights into auxiliary cofactor usage by radical S-adenosylmethionine enzymes."],"pmcid":["PMC10197145"],"funding_grant_id":["R35 GM119707","GM119707","MCB -1158486"],"pubmed_authors":["Jeyachandran VR","Boal AK"],"additional_accession":[]},"is_claimable":false,"name":"Structural insights into auxiliary cofactor usage by radical S-adenosylmethionine enzymes.","description":"Radical S-adenosylmethionine (SAM) enzymes use a common catalytic core for diverse transformations. While all radical SAM enzymes bind a Fe<sub>4</sub>S<sub>4</sub> cluster via a characteristic tri-cysteine motif, many bind additional metal cofactors. Recently reported structures of radical SAM enzymes that use methylcobalamin or additional iron-sulfur clusters as cosubstrates show that these auxiliary units are anchored by N- and C-terminal domains that vary significantly in size and topology. Despite this architectural diversity, all use a common surface for auxiliary cofactor docking. In the sulfur insertion and metallocofactor assembly systems evaluated here, interaction with iron-sulfur cluster assembly proteins or downstream scaffold proteins is an important component of catalysis. S","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jun","modification":"2025-04-21T23:46:22.145Z","creation":"2025-04-05T19:15:10.015Z"},"accession":"S-EPMC10197145","cross_references":{"pubmed":["35512465"],"doi":["10.1016/j.cbpa.2022.102153"]}}