2zpt
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:2zpt.jpg|left|200px]] | ||
| - | < | + | ==Crystal structure of mouse sulfotransferase SULT1D1 complex with PAP== |
| - | + | <StructureSection load='2zpt' size='340' side='right'caption='[[2zpt]], [[Resolution|resolution]] 1.15Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2zpt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZPT FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15Å</td></tr> | |
| - | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zpt OCA], [https://pdbe.org/2zpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zpt RCSB], [https://www.ebi.ac.uk/pdbsum/2zpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zpt ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ST1D1_MOUSE ST1D1_MOUSE] Sulfotransferase with broad substrate specificity that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, such as dopamine, prostaglandins, leukotriene E4, drugs and xenobiotic compounds. Has sulfotransferase activity towards p-nitrophenol, 2-naphthylamine and minoxidil (in vitro). Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites.<ref>PMID:15087475</ref> <ref>PMID:18977225</ref> <ref>PMID:19966186</ref> <ref>PMID:9647753</ref> <ref>PMID:9920733</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zp/2zpt_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zpt ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In mammals, sulfonation as mediated by specific cytosolic sulfotransferases (SULTs) plays an important role in the homeostasis of dopamine and other catecholamines. To gain insight into the structural basis for dopamine recognition/binding, we determined the crystal structure of a mouse dopamine-sulfating SULT, mouse SULT1D1 (mSULT1D1). Data obtained indicated that mSULT1D1 comprises of a single alpha/beta domain with a five-stranded parallel beta-sheet. In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. These results imply differences in substrate binding between dopamine-sulfating SULTs from different species. | ||
| - | + | Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase.,Teramoto T, Sakakibara Y, Inada K, Kurogi K, Liu MC, Suiko M, Kimura M, Kakuta Y FEBS Lett. 2008 Nov 26;582(28):3909-14. Epub 2008 Oct 31. PMID:18977225<ref>PMID:18977225</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2zpt" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Large Structures]] |
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| - | == | + | |
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | + | [[Category: Inada K]] | |
| - | + | [[Category: Kakuta Y]] | |
| - | [[Category: Inada | + | [[Category: Kimura M]] |
| - | [[Category: Kakuta | + | [[Category: Liu MC]] |
| - | [[Category: Kimura | + | [[Category: Sakakibara Y]] |
| - | [[Category: Liu | + | [[Category: Suiko M]] |
| - | [[Category: Sakakibara | + | [[Category: Teramoto T]] |
| - | [[Category: Suiko | + | |
| - | [[Category: Teramoto | + | |
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Current revision
Crystal structure of mouse sulfotransferase SULT1D1 complex with PAP
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Categories: Large Structures | Mus musculus | Inada K | Kakuta Y | Kimura M | Liu MC | Sakakibara Y | Suiko M | Teramoto T
