| Structural highlights
2zyv is a 1 chain structure with sequence from Mus musculus. 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: | , ,
| | Related: | 2zpt, 2zvp, 2zvq, 2zyt, 2zyu, 2zyw |
| Gene: | Sult1d1 (Mus musculus) |
| Activity: | Tyrosine-ester sulfotransferase, with EC number 2.8.2.9 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Teramoto T, Sakakibara Y, Liu MC, 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. 2009 May 22;383(1):83-7. Epub 2009 Apr 1. PMID:19344693 doi:http://dx.doi.org/10.1016/j.bbrc.2009.03.146
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