Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis.
FeS 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.
Clausen
T
T
Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried, Germany. clausen@biochem.mpg.de
Kaiser
J T
JT
Steegborn
C
C
Huber
R
R
Kessler
D
D
D000595:Amino Acid Sequence; D013437:Carbon-Sulfur Lyases / Q000737:chemistry*; D018360:Crystallography, X-Ray; D000458:Cyanobacteria / Q000201:enzymology*; D003545:Cysteine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D004220:Disulfides / Q000737:chemistry* / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000096:biosynthesis*; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry; D017510:Protein Folding
D004220:Disulfides; D007506:Iron-Sulfur Proteins; D009842:Oligopeptides; C116840:cysteine persulfide; D013437:Carbon-Sulfur Lyases; C105473:L-cysteine-cystine C-S lyase; D003545:Cysteine