2ZYV
Crystal structure of mouse cytosolic sulfotransferase mSULT1D1 complex with PAPS/PAP and p-nitrophenol
Summary for 2ZYV
| Entry DOI | 10.2210/pdb2zyv/pdb |
| Related | 2ZPT 2ZVP 2ZVQ 2ZYT 2ZYU 2ZYW |
| Descriptor | Tyrosine-ester sulfotransferase, 3'-PHOSPHATE-ADENOSINE-5'-PHOSPHATE SULFATE, P-NITROPHENOL, ... (5 entities in total) |
| Functional Keywords | sult1d1, sult, sulfotransferase, paps, p-nitrophenol, michaelis complex, sulfonation mechanism, transferase |
| Biological source | Mus musculus (mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 36466.34 |
| Authors | Teramoto, T.,Sakakibara, Y.,Liu, M.-C.,Suiko, M.,Kimura, M.,Kakuta, Y. (deposition date: 2009-01-29, release date: 2009-04-21, Last modification date: 2023-11-01) |
| Primary citation | Teramoto, T.,Sakakibara, Y.,Liu, M.-C.,Suiko, M.,Kimura, M.,Kakuta, Y. Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate Biochem.Biophys.Res.Commun., 383:83-87, 2009 Cited by PubMed Abstract: 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. PubMed: 19344693DOI: 10.1016/j.bbrc.2009.03.146 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.81 Å) |
Structure validation
Download full validation report
