5x2b | pdb_00005x2b

Crystal structure of mouse sulfotransferase SULT7A1 complexed with PAP

spinqualitylabelsall models 5x2b, resolution 2.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5x2b is a 12 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 2.08Å Ligands: A3P, CA, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7ZWN4_MOUSE Publication Abstract from PubMed Cytosolic sulfotransferases (SULTs) are cytosolic enzymes that catalyze the transfer of sulfonate group to key endogenous compounds, altering the physiological functions of their substrates. SULT enzymes catalyze the O-sulfonation of hydroxy groups or N-sulfonation of amino groups of substrate compounds. In this study, we report the discovery of C-sulfonation of alpha,beta-unsaturated carbonyl groups mediated by a new SULT enzyme, SULT7A1, and human SULT1C4. Enzymatic assays revealed that SULT7A1 is capable of transferring the sulfonate group from 3'-phosphoadenosine 5'-phosphosulfate to the alpha-carbon of alpha,beta-unsaturated carbonyl-containing compounds, including cyclopentenone prostaglandins as representative endogenous substrates. Structural analyses of SULT7A1 suggest that the C-sulfonation reaction is catalyzed by a novel mechanism mediated by His and Cys residues in the active site. Ligand-activity assays demonstrated that sulfonated 15-deoxy prostaglandin J(2) exhibits antagonist activity against the prostaglandin receptor EP2 and the prostacyclin receptor IP. Modification of alpha,beta-unsaturated carbonyl groups via the new prostaglandin-sulfonating enzyme, SULT7A1, may regulate the physiological function of prostaglandins in the gut. Discovery of C-sulfonation of alpha,beta-unsaturated carbonyl groups will broaden the spectrum of potential substrates and physiological functions of SULTs. A new type of sulfation reaction: C-sulfonation for alpha,beta-unsaturated carbonyl groups by a novel sulfotransferase SULT7A1.,Kurogi K, Sakakibara Y, Hashiguchi T, Kakuta Y, Kanekiyo M, Teramoto T, Fukushima T, Bamba T, Matsumoto J, Fukusaki E, Kataoka H, Suiko M PNAS Nexus. 2024 Mar 4;3(3):pgae097. doi: 10.1093/pnasnexus/pgae097. eCollection , 2024 Mar. PMID:38487162 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sulfotransferase 3D structures

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