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pubmed-article:10760256pubmed:abstractTextFeS 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.lld:pubmed
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pubmed-article:10760256pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:10760256pubmed:articleTitleCrystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis.lld:pubmed
pubmed-article:10760256pubmed:affiliationMax-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried, Germany. clausen@biochem.mpg.delld:pubmed
pubmed-article:10760256pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10760256pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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