1dp2: Difference between revisions

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[[Image:1dp2.~~jpg~~|left|200px]]

[[Image:1dp2.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RHODANESE AND LIPOATE~~'''~~

===CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RHODANESE AND LIPOATE===

~~==Overview==~~

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~~Dihydrolipoate is an acceptor of the rhodanese-bound sulfane sulfur atom~~, ~~as shown by analysis of~~ the ~~elementary steps of~~ the ~~reaction catalyzed by rhodanese~~. The crystal structure of sulfur-substituted rhodanese complexed with the non-reactive oxidized form of lipoate has revealed that the compound is bound at the enzyme active site, with the dithiolane ring buried in the interior of the cavity and the carboxylic end pointing towards the solvent. ~~One of the sulfur atoms of the ligand in the unproductive complex is relatively close to the sulfane sulfur bound to Cys-247~~, ~~the sulfur that~~ is ~~transferred during~~ the ~~catalytic reaction~~. ~~This mode of binding of lipoate is likely to mimic that of dihydrolipoate. The results presented here support the possible role of dihydrolipoate as sulfur~~-~~acceptor substrate of rhodanese in an enzymatic reaction that might serve to provide iron~~-~~sulfur proteins with inorganic sulfide.~~

The line below this paragraph, {{ABSTRACT_PUBMED_11004580}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11004580 is the PubMed ID number.

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==About this Structure==

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[[Category: Rhodanese]]

[[Category: Sulfurtransferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 14~~:06:09 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:24:04 2008''

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-[[Image:1dp2.jpg|left|200px]]
+{{Seed}}
+[[Image:1dp2.png|left|200px]]
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 {{STRUCTURE_1dp2|  PDB=1dp2  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RHODANESE AND LIPOATE'''
+===CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RHODANESE AND LIPOATE===
-==Overview==
+<!--
-Dihydrolipoate is an acceptor of the rhodanese-bound sulfane sulfur atom, as shown by analysis of the elementary steps of the reaction catalyzed by rhodanese. The crystal structure of sulfur-substituted rhodanese complexed with the non-reactive oxidized form of lipoate has revealed that the compound is bound at the enzyme active site, with the dithiolane ring buried in the interior of the cavity and the carboxylic end pointing towards the solvent. One of the sulfur atoms of the ligand in the unproductive complex is relatively close to the sulfane sulfur bound to Cys-247, the sulfur that is transferred during the catalytic reaction. This mode of binding of lipoate is likely to mimic that of dihydrolipoate. The results presented here support the possible role of dihydrolipoate as sulfur-acceptor substrate of rhodanese in an enzymatic reaction that might serve to provide iron-sulfur proteins with inorganic sulfide.
+The line below this paragraph, {{ABSTRACT_PUBMED_11004580}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11004580 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11004580}}
 ==About this Structure==
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 [[Category: Rhodanese]]
 [[Category: Sulfurtransferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:06:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:24:04 2008''