5MEX

Sulphotransferase-18 from Arabidopsis thaliana in complex with 3'-phosphoadenosine 5'-phosphate (PAP)and sinigrin

5MEX の概要

• エントリーDOI: 10.2210/pdb5mex/pdb
• 分子名称: Cytosolic sulfotransferase 18, 3'-PHOSPHATE-ADENOSINE-5'-DIPHOSPHATE, Sinigrin, ... (6 entities in total)
• 機能のキーワード: sulphotransferases, glucosinolate-biosynthesis, catalysis, transferase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• 細胞内の位置: Cytoplasm : Q9C9C9
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39076.86

構造登録者

Hirschmann, F.,Krause, F.,Baruch, P.,Chizhov, I.,Mueller, J.W.,Manstein, D.J.,Papenbrock, J.,Fedorov, R. (登録日: 2016-11-16, 公開日: 2017-07-05, 最終更新日: 2024-01-17)

主引用文献

Hirschmann, F.,Krause, F.,Baruch, P.,Chizhov, I.,Mueller, J.W.,Manstein, D.J.,Papenbrock, J.,Fedorov, R.
Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism.
Sci Rep, 7:4160-4160, 2017

PubMed Abstract: Sulphotransferases 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.

PubMed: 28646214
DOI: 10.1038/s41598-017-04539-2

実験手法

X-RAY DIFFRACTION (1.92 Å)