2zyv | pdb_00002zyv

Crystal structure of mouse cytosolic sulfotransferase mSULT1D1 complex with PAPS/PAP and p-nitrophenol

spinqualitylabelsall models 2zyv, resolution 1.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zyv is a 1 chain structure with sequence from Lk3 transgenic mice. The August 2009 RCSB PDB Molecule of the Month feature on Sulfotransferases by David Goodsell is 10.2210/rcsb_pdb/mom_2009_8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, NPO, PPS Related: 2zpt, 2zvp, 2zvq, 2zyt, 2zyu, 2zyw 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. 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 We report the crystal structure of mouse sulfotransferase, mSULT1D1, complexed with donor substrate 3'-phosphoadenosine 5'-phosphosulfate and accepter substrate p-nitrophenol. The structure is the first report of the native Michaelis complex of sulfotransferase. In the structure, three proposed catalytic residues (Lys48, Lys106, and His108) were in proper positions for engaging in the sulfuryl transfer reaction. The data strongly support that the sulfuryl transfer reaction proceeds through an S(N)2-like in-line displacement mechanism. Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate.,Teramoto T, Sakakibara Y, Liu MC, Suiko M, Kimura M, Kakuta Y Biochem Biophys Res Commun. 2009 May 22;383(1):83-7. Epub 2009 Apr 1. PMID:19344693 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sulfotransferase

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