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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2000-5-17
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-10406803,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-10468587,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-15299354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-15299723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-2615765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-7748903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-8161529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-8377180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-8425548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-8464885,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-8482384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-8905231,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-9099686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-9235882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-9278392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-9582371,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-9667933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-9738949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-9757107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-9813017,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-9867829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10760256-9914259
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
97
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3856-61
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10760256-Amino Acid Sequence,
pubmed-meshheading:10760256-Carbon-Sulfur Lyases,
pubmed-meshheading:10760256-Crystallography, X-Ray,
pubmed-meshheading:10760256-Cyanobacteria,
pubmed-meshheading:10760256-Cysteine,
pubmed-meshheading:10760256-Disulfides,
pubmed-meshheading:10760256-Iron-Sulfur Proteins,
pubmed-meshheading:10760256-Models, Molecular,
pubmed-meshheading:10760256-Oligopeptides,
pubmed-meshheading:10760256-Protein Folding
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pubmed:year |
2000
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pubmed:articleTitle |
Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis.
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pubmed:affiliation |
Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried, Germany. clausen@biochem.mpg.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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