5BRQ

Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA)

5BRQ の概要

• エントリーDOI: 10.2210/pdb5brq/pdb
• 関連するPDBエントリー: 5BRP
• 分子名称: Glycoside Hydrolase Family 13, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: trehalose-6-phosphate hydrolase, tim barrel, gh13 family, hydrolase
• 由来する生物種: Bacillus licheniformis ATCC 14580 = DSM 13
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 266666.47

構造登録者

Hsiao, C.-D.,Lin, M.-G. (登録日: 2015-06-01, 公開日: 2016-03-02, 最終更新日: 2023-11-08)

主引用文献

Lin, M.-G.,Chi, M.-C.,Naveen, V.,Li, Y.-C.,Lin, L.-L.,Hsiao, C.-D.
Bacillus licheniformis trehalose-6-phosphate hydrolase structures suggest keys to substrate specificity
Acta Crystallogr D Struct Biol, 72:59-70, 2016

PubMed Abstract: Trehalose-6-phosphate hydrolase (TreA) belongs to glycoside hydrolase family 13 (GH13) and catalyzes the hydrolysis of trehalose 6-phosphate (T6P) to yield glucose and glucose 6-phosphate. The products of this reaction can be further metabolized by the energy-generating glycolytic pathway. Here, crystal structures of Bacillus licheniformis TreA (BlTreA) and its R201Q mutant complexed with p-nitrophenyl-α-D-glucopyranoside (R201Q-pPNG) are presented at 2.0 and 2.05 Å resolution, respectively. The overall structure of BlTreA is similar to those of other GH13 family enzymes. However, detailed structural comparisons revealed that the catalytic site of BlTreA contains a long loop that adopts a different conformation from those of other GH13 family members. Unlike the homologous regions of Bacillus cereus oligo-1,6-glucosidase (BcOgl) and Erwinia rhapontici isomaltulose synthase (NX-5), the surface potential of the BlTreA active site exhibits a largely positive charge contributed by the four basic residues His281, His282, Lys284 and Lys292. Mutation of these residues resulted in significant decreases in the enzymatic activity of BlTreA. Strikingly, the (281)HHLK(284) motif and Lys292 play critical roles in substrate discrimination by BlTreA.

PubMed: 26894535
DOI: 10.1107/S2059798315020756

実験手法

X-RAY DIFFRACTION (2.003 Å)