1elu: Difference between revisions

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[[Image:1elu.~~gif~~|left|200px]]

[[Image:1elu.png|left|200px]]

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~~'''~~COMPLEX BETWEEN THE CYSTINE C-S LYASE C-DES AND ITS REACTION PRODUCT CYSTEINE PERSULFIDE.~~'''~~

===COMPLEX BETWEEN THE CYSTINE C-S LYASE C-DES AND ITS REACTION PRODUCT CYSTEINE PERSULFIDE.===

~~==Overview==~~

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~~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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10760256}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10760256 is the PubMed ID number.

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==About this Structure==

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[[Category: Pyridoxal 5'-phosphate]]

[[Category: Thiocysteine]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:15:33 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:57:23 2008''

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-[[Image:1elu.gif|left|200px]]
+{{Seed}}
+[[Image:1elu.png|left|200px]]
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 {{STRUCTURE_1elu|  PDB=1elu  |  SCENE=  }}
-'''COMPLEX BETWEEN THE CYSTINE C-S LYASE C-DES AND ITS REACTION PRODUCT CYSTEINE PERSULFIDE.'''
+===COMPLEX BETWEEN THE CYSTINE C-S LYASE C-DES AND ITS REACTION PRODUCT CYSTEINE PERSULFIDE.===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10760256}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10760256 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10760256}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Pyridoxal 5'-phosphate]]
 [[Category: Thiocysteine]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:15:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:57:23 2008''