1dp2: Difference between revisions

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New page: left|200px<br /><applet load="1dp2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dp2, resolution 2.01Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1dp2.jpg|left|200px]]<br /><applet load="1dp2" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dp2.jpg|left|200px]]<br /><applet load="1dp2" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dp2, resolution 2.01&Aring;" />
caption="1dp2, resolution 2.01&Aring;" />
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RHODANESE AND LIPOATE'''<br />
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RHODANESE AND LIPOATE'''<br />


==Overview==
==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.
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.


==About this Structure==
==About this Structure==
1DP2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with LPA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Thiosulfate_sulfurtransferase Thiosulfate sulfurtransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.1 2.8.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DP2 OCA].  
1DP2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=LPA:'>LPA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Thiosulfate_sulfurtransferase Thiosulfate sulfurtransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.1 2.8.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DP2 OCA].  


==Reference==
==Reference==
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[[Category: sulfurtransferase]]
[[Category: sulfurtransferase]]


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Revision as of 13:18, 21 February 2008

File:1dp2.jpg


1dp2, resolution 2.01Å

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CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RHODANESE AND LIPOATE

OverviewOverview

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.

About this StructureAbout this Structure

1DP2 is a Single protein structure of sequence from Bos taurus with as ligand. Active as Thiosulfate sulfurtransferase, with EC number 2.8.1.1 Full crystallographic information is available from OCA.

ReferenceReference

Specific interaction of lipoate at the active site of rhodanese., Cianci M, Gliubich F, Zanotti G, Berni R, Biochim Biophys Acta. 2000 Aug 31;1481(1):103-8. PMID:11004580

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