5X2B
Crystal structure of mouse sulfotransferase SULT7A1 complexed with PAP
Summary for 5X2B
| Entry DOI | 10.2210/pdb5x2b/pdb |
| Descriptor | Sulfotransferase, ADENOSINE-3'-5'-DIPHOSPHATE, CALCIUM ION, ... (7 entities in total) |
| Functional Keywords | transferase |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 12 |
| Total formula weight | 397615.47 |
| Authors | Kanekiyo, M.,Teramoto, T.,Kakuta, Y. (deposition date: 2017-01-31, release date: 2018-03-28, Last modification date: 2025-03-19) |
| Primary citation | Kurogi, K.,Sakakibara, Y.,Hashiguchi, T.,Kakuta, Y.,Kanekiyo, M.,Teramoto, T.,Fukushima, T.,Bamba, T.,Matsumoto, J.,Fukusaki, E.,Kataoka, H.,Suiko, M. A new type of sulfation reaction: C -sulfonation for alpha , beta-unsaturated carbonyl groups by a novel sulfotransferase SULT7A1. Pnas Nexus, 3:pgae097-pgae097, 2024 Cited by PubMed Abstract: 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 -sulfonation of hydroxy groups or -sulfonation of amino groups of substrate compounds. In this study, we report the discovery of -sulfonation of α,β-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 α-carbon of α,β-unsaturated carbonyl-containing compounds, including cyclopentenone prostaglandins as representative endogenous substrates. Structural analyses of SULT7A1 suggest that the -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 exhibits antagonist activity against the prostaglandin receptor EP2 and the prostacyclin receptor IP. Modification of α,β-unsaturated carbonyl groups via the new prostaglandin-sulfonating enzyme, SULT7A1, may regulate the physiological function of prostaglandins in the gut. Discovery of -sulfonation of α,β-unsaturated carbonyl groups will broaden the spectrum of potential substrates and physiological functions of SULTs. PubMed: 38487162DOI: 10.1093/pnasnexus/pgae097 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.08 Å) |
Structure validation
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