2zvq

Crystal structure of mouse cytosolic sulfotransferase mSULT1D1 complex with PAP and alpha-naphtholCrystal structure of mouse cytosolic sulfotransferase mSULT1D1 complex with PAP and alpha-naphthol

Structural highlights

2zvq is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.3Å
Ligands:	, ,
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

The mouse cytosolic sulfotransferase, mSULT1D1, catalyzes the sulfonation of a wide range of phenolic molecules including p-nitrophenol (pNP), alpha-naphthol (alphaNT), serotonin, as well as dopamine and its metabolites. To gain insight into the structural basis for its broad range substrate specificity, we solved two distinct ternary crystal structures of mSULT1D1, complexed with 3'-phosphoadenosine-5'-phosphate (PAP) plus pNP or PAP plus alphaNT. The structures revealed that the mSULT1D1 contains an L-shaped accepter-binding site which comprises 20 amino acid residues and four conserved water molecules. The shape of the accepter-binding site can be adjusted by conformational changes of two residues, Ile148 and Glu247, upon binding with respective substrates.

Structural basis for the broad range substrate specificity of a novel mouse cytosolic sulfotransferase--mSULT1D1.,Teramoto T, Sakakibara Y, Liu MC, Suiko M, Kimura M, Kakuta Y Biochem Biophys Res Commun. 2009 Jan 30;379(1):76-80. Epub 2008 Dec 13. PMID:19073143^[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, Liu MC, Suiko M, Kimura M, Kakuta Y. Structural basis for the broad range substrate specificity of a novel mouse cytosolic sulfotransferase--mSULT1D1. Biochem Biophys Res Commun. 2009 Jan 30;379(1):76-80. Epub 2008 Dec 13. PMID:19073143 doi:10.1016/j.bbrc.2008.12.013

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OCA

[1] 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

[2] 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

[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

[4] 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

[5] 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

[6] Teramoto T, Sakakibara Y, Liu MC, Suiko M, Kimura M, Kakuta Y. Structural basis for the broad range substrate specificity of a novel mouse cytosolic sulfotransferase--mSULT1D1. Biochem Biophys Res Commun. 2009 Jan 30;379(1):76-80. Epub 2008 Dec 13. PMID:19073143 doi:10.1016/j.bbrc.2008.12.013

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