1elq: Difference between revisions
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'''CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES''' | '''CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES''' | ||
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[[Category: Kessler, D.]] | [[Category: Kessler, D.]] | ||
[[Category: Steegborn, C.]] | [[Category: Steegborn, C.]] | ||
[[Category: | [[Category: Fes cluster biosynthesis]] | ||
[[Category: | [[Category: Nif]] | ||
[[Category: | [[Category: Pyridoxal 5'-phosphate]] | ||
[[Category: | [[Category: Thiocysteine]] | ||
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Revision as of 15:15, 2 May 2008
CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES
OverviewOverview
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.
About this StructureAbout this Structure
1ELQ is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis., Clausen T, Kaiser JT, Steegborn C, Huber R, Kessler D, Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):3856-61. PMID:10760256 Page seeded by OCA on Fri May 2 15:15:15 2008