1dp2: Difference between revisions
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[[Image:1dp2.jpg|left|200px]] | [[Image:1dp2.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RHODANESE AND LIPOATE''' | {{Structure | ||
|PDB= 1dp2 |SIZE=350|CAPTION= <scene name='initialview01'>1dp2</scene>, resolution 2.01Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=LPA:LIPOIC ACID'>LPA</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RHODANESE AND LIPOATE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DP2 is a [ | 1DP2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DP2 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11004580 11004580] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sulfurtransferase]] | [[Category: sulfurtransferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:42:03 2008'' | ||
Revision as of 11:42, 20 March 2008
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| , resolution 2.01Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Thiosulfate sulfurtransferase, with EC number 2.8.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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