5mek
Sulphotransferase-18 from Arabidopsis thaliana in complex with 3'-phosphoadenosine 5'-phosphate (PAP)
Structural highlights
FunctionSOT18_ARATH Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of desulfo-glucosinolates (dsGSs), the final step in the biosynthesis of the glucosinolate core structure. Preferred substrate are the long-chain desulfo-glucosinolates, 7-methylthioheptyl and 8-methylthiooctyl, derived from methionine. Substrate preference is desulfo-benzyl glucosinolate > desulfo-4-methylthiobutyl glucosinolate > desulfo-6-methylthiohexyl glucosinolate > desulfo-3-methylthiopropyl glucosinolate > desulfo-indol-3-yl methyl glucosinolate > desulfo-singrin > desulfo-3-butenyl glucosinolate.[1] [2] [3] [4] [5] Publication Abstract from PubMedSulphotransferases are a diverse group of enzymes catalysing the transfer of a sulfuryl group from 3'-phosphoadenosine 5'-phosphosulphate (PAPS) to a broad range of secondary metabolites. They exist in all kingdoms of life. In Arabidopsis thaliana (L.) Heynh. twenty-two sulphotransferase (SOT) isoforms were identified. Three of those are involved in glucosinolate (Gl) biosynthesis, glycosylated sulphur-containing aldoximes containing chemically different side chains, whose break-down products are involved in stress response against herbivores, pathogens, and abiotic stress. To explain the differences in substrate specificity of desulpho (ds)-Gl SOTs and to understand the reaction mechanism of plant SOTs, we determined the first high-resolution crystal structure of the plant ds-Gl SOT AtSOT18 in complex with 3'-phosphoadenosine 5'-phosphate (PAP) alone and together with the Gl sinigrin. These new structural insights into the determination of substrate specificity were complemented by mutagenesis studies. The structure of AtSOT18 invigorates the similarity between plant and mammalian sulphotransferases, which illustrates the evolutionary conservation of this multifunctional enzyme family. We identified the essential residues for substrate binding and catalysis and demonstrated that the catalytic mechanism is conserved between human and plant enzymes. Our study indicates that the loop-gating mechanism is likely to be a source of the substrate specificity in plants. Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism.,Hirschmann F, Krause F, Baruch P, Chizhov I, Mueller JW, Manstein DJ, Papenbrock J, Fedorov R Sci Rep. 2017 Jun 23;7(1):4160. doi: 10.1038/s41598-017-04539-2. PMID:28646214[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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