2zpt

From Proteopedia

(Difference between revisions)

Revision as of 21:54, 5 August 2016

Crystal structure of mouse sulfotransferase SULT1D1 complex with PAP

Structural highlights

2zpt is a 1 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	Sult1d1 (LK3 transgenic mice)
Activity:	Tyrosine-ester sulfotransferase, with EC number 2.8.2.9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shimada M, Terazawa R, Kamiyama Y, Honma W, Nagata K, Yamazoe Y. Unique properties of a renal sulfotransferase, St1d1, in dopamine metabolism. J Pharmacol Exp Ther. 2004 Aug;310(2):808-14. Epub 2004 Apr 15. PMID:15087475 doi:http://dx.doi.org/10.1124/jpet.104.065532
↑ Teramoto T, Sakakibara Y, Inada K, Kurogi K, Liu MC, Suiko M, Kimura M, Kakuta Y. Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase. FEBS Lett. 2008 Nov 26;582(28):3909-14. Epub 2008 Oct 31. PMID:18977225 doi:S0014-5793(08)00867-3
↑ Wong S, Tan K, Carey KT, Fukushima A, Tiganis T, Cole TJ. Glucocorticoids stimulate hepatic and renal catecholamine inactivation by direct rapid induction of the dopamine sulfotransferase Sult1d1. Endocrinology. 2010 Jan;151(1):185-94. doi: 10.1210/en.2009-0590. Epub 2009 Dec, 4. PMID:19966186 doi:http://dx.doi.org/10.1210/en.2009-0590
↑ Sakakibara Y, Yanagisawa K, Takami Y, Nakayama T, Suiko M, Liu MC. Molecular cloning, expression, and functional characterization of novel mouse sulfotransferases. Biochem Biophys Res Commun. 1998 Jun 29;247(3):681-6. PMID:9647753 doi:http://dx.doi.org/10.1006/bbrc.1998.8872
↑ Liu MC, Sakakibara Y, Liu CC. Bacterial expression, purification, and characterization of a novel mouse sulfotransferase that catalyzes the sulfation of eicosanoids. Biochem Biophys Res Commun. 1999 Jan 8;254(1):65-9. PMID:9920733 doi:http://dx.doi.org/10.1006/bbrc.1998.9872
↑ Teramoto T, Sakakibara Y, Inada K, Kurogi K, Liu MC, Suiko M, Kimura M, Kakuta Y. Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase. FEBS Lett. 2008 Nov 26;582(28):3909-14. Epub 2008 Oct 31. PMID:18977225 doi:S0014-5793(08)00867-3

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2zpt"

@@ Line 1: / Line 1: @@
 ==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 [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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZPT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2zpt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZPT FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sult1d1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sult1d1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosine-ester_sulfotransferase Tyrosine-ester sulfotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.2.9 2.8.2.9] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zpt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zpt RCSB], [http://www.ebi.ac.uk/pdbsum/2zpt PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zpt OCA], [http://pdbe.org/2zpt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zpt RCSB], [http://www.ebi.ac.uk/pdbsum/2zpt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zpt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q9R2C2_MOUSE Q9R2C2_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:9647753</ref> <ref>PMID:9920733</ref> <ref>PMID:15087475</ref> <ref>PMID:19966186</ref> <ref>PMID:18977225</ref>
+[[http://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]]
@@ Line 18: / Line 19: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2zpt" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 35: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Mus musculus]]
+[[Category: Lk3 transgenic mice]]
 [[Category: Tyrosine-ester sulfotransferase]]
 [[Category: Inada, K]]

2zpt

From Proteopedia

Revision as of 21:54, 5 August 2016

Crystal structure of mouse sulfotransferase SULT1D1 complex with PAP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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