PubMed:10760256 JSONTXT

{"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":0,"end":129},"obj":"Sentence"},{"id":"T2","span":{"begin":130,"end":252},"obj":"Sentence"},{"id":"T3","span":{"begin":253,"end":367},"obj":"Sentence"},{"id":"T4","span":{"begin":368,"end":532},"obj":"Sentence"},{"id":"T5","span":{"begin":533,"end":615},"obj":"Sentence"},{"id":"T6","span":{"begin":616,"end":764},"obj":"Sentence"},{"id":"T7","span":{"begin":765,"end":999},"obj":"Sentence"}],"text":"Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis.\nFeS clusters are versatile cofactors of a variety of proteins, but the mechanisms of their biosynthesis are still unknown. The cystine C-S lyase from Synechocystis has been identified as a participant in ferredoxin FeS cluster formation. Herein, we report on the crystal structure of the lyase and of a complex with the reaction products of cystine cleavage at 1.8- and 1.55-A resolution, respectively. The sulfur-containing product was unequivocally identified as cysteine persulfide. The reactive persulfide group is fixed by a hydrogen bond to His-114 in the center of a hydrophobic pocket and is thereby shielded from the solvent. Binding and stabilization of the cysteine persulfide represent an alternative to the generation of a protein-bound persulfide by NifS-like proteins and point to the general importance of persulfidic compounds for FeS cluster assembly."}