pubmed-article:10760256 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10760256 | lifeskim:mentions | umls-concept:C0995537 | lld:lifeskim |
pubmed-article:10760256 | lifeskim:mentions | umls-concept:C0010682 | lld:lifeskim |
pubmed-article:10760256 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:10760256 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:10760256 | lifeskim:mentions | umls-concept:C1704332 | lld:lifeskim |
pubmed-article:10760256 | lifeskim:mentions | umls-concept:C1096814 | lld:lifeskim |
pubmed-article:10760256 | lifeskim:mentions | umls-concept:C0762486 | lld:lifeskim |
pubmed-article:10760256 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:10760256 | pubmed:dateCreated | 2000-5-17 | lld:pubmed |
pubmed-article:10760256 | 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. | lld:pubmed |
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pubmed-article:10760256 | pubmed:language | eng | lld:pubmed |
pubmed-article:10760256 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10760256 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10760256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10760256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10760256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10760256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10760256 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10760256 | pubmed:month | Apr | lld:pubmed |
pubmed-article:10760256 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:10760256 | pubmed:author | pubmed-author:HuberRR | lld:pubmed |
pubmed-article:10760256 | pubmed:author | pubmed-author:ClausenTT | lld:pubmed |
pubmed-article:10760256 | pubmed:author | pubmed-author:KesslerDD | lld:pubmed |
pubmed-article:10760256 | pubmed:author | pubmed-author:KaiserJ TJT | lld:pubmed |
pubmed-article:10760256 | pubmed:author | pubmed-author:SteegbornCC | lld:pubmed |
pubmed-article:10760256 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10760256 | pubmed:day | 11 | lld:pubmed |
pubmed-article:10760256 | pubmed:volume | 97 | lld:pubmed |
pubmed-article:10760256 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10760256 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10760256 | pubmed:pagination | 3856-61 | lld:pubmed |
pubmed-article:10760256 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:10760256 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10760256 | pubmed:articleTitle | Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis. | lld:pubmed |
pubmed-article:10760256 | pubmed:affiliation | Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried, Germany. clausen@biochem.mpg.de | lld:pubmed |
pubmed-article:10760256 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10760256 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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