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[[Image:2zpt.png|left|200px]]


{{STRUCTURE_2zpt| PDB=2zpt | SCENE= }}
==Crystal structure of mouse sulfotransferase SULT1D1 complex with PAP==
<StructureSection load='2zpt' size='340' side='right'caption='[[2zpt]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== 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]] 1.15&#8491;</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 mouse sulfotransferase SULT1D1 complex with PAP===
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>


{{ABSTRACT_PUBMED_18977225}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2zpt" style="background-color:#fffaf0;"></div>
[[2zpt]] is a 1 chain structure of [[Sulfotransferase]] with sequence from [http://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].


==See Also==
==See Also==
*[[Sulfotransferase|Sulfotransferase]]
*[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:018977225</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Tyrosine-ester sulfotransferase]]
[[Category: Inada K]]
[[Category: Inada, K.]]
[[Category: Kakuta Y]]
[[Category: Kakuta, Y.]]
[[Category: Kimura M]]
[[Category: Kimura, M.]]
[[Category: Liu MC]]
[[Category: Liu, M C.]]
[[Category: Sakakibara Y]]
[[Category: Sakakibara, Y.]]
[[Category: Suiko M]]
[[Category: Suiko, M.]]
[[Category: Teramoto T]]
[[Category: Teramoto, T.]]
[[Category: Catecholamine]]
[[Category: Sulfonation]]
[[Category: Sulfotransferase]]
[[Category: Sult1d1]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/2zpt"