2ZPT
Crystal structure of mouse sulfotransferase SULT1D1 complex with PAP
Summary for 2ZPT
| Entry DOI | 10.2210/pdb2zpt/pdb |
| Descriptor | Tyrosine-ester sulfotransferase, ADENOSINE-3'-5'-DIPHOSPHATE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | sult1d1, catecholamine, sulfotransferase, sulfonation, transferase |
| Biological source | Mus musculus (mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 35647.59 |
| Authors | Teramoto, T.,Sakakibara, Y.,Inada, K.,Liu, M.C.,Suiko, M.,Kimura, M.,Kakuta, Y. (deposition date: 2008-07-28, release date: 2008-11-18, Last modification date: 2023-11-01) |
| Primary citation | Teramoto, T.,Sakakibara, Y.,Inada, K.,Kurogi, K.,Liu, M.-C.,Suiko, M.,Kimura, M.,Kakuta, Y. Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase Febs Lett., 582:3909-3914, 2008 Cited by PubMed Abstract: 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. PubMed: 18977225DOI: 10.1016/j.febslet.2008.10.035 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
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