5YQS

Isoprimeverose-producing enzyme from Aspergillus oryzae in complex with isoprimeverose

5YQS の概要

• エントリーDOI: 10.2210/pdb5yqs/pdb
• 分子名称: Isoprimeverose-producing enzyme, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-xylopyranose-(1-6)-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: glycoside hydrolase family 3, hydrolase
• 由来する生物種: Aspergillus oryzae RIB40 (Yellow koji mold)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 174845.89

構造登録者

Yaoi, K.,Matsuzawa, T.,Watanabe, M.,Nakamichi, Y. (登録日: 2017-11-07, 公開日: 2018-11-14, 最終更新日: 2024-10-23)

主引用文献

Matsuzawa, T.,Watanabe, M.,Nakamichi, Y.,Fujimoto, Z.,Yaoi, K.
Crystal structure and substrate recognition mechanism of Aspergillus oryzae isoprimeverose-producing enzyme.
J.Struct.Biol., 205:84-90, 2019

PubMed Abstract: Isoprimeverose-producing enzymes (IPases) release isoprimeverose (α-d-xylopyranosyl-(1 → 6)-d-glucopyranose) from the non-reducing end of xyloglucan oligosaccharides. Aspergillus oryzae IPase (IpeA) is classified as a member of the glycoside hydrolase family 3 (GH3); however, it has unusual substrate specificity compared with other GH3 enzymes. Xylopyranosyl branching at the non-reducing ends of xyloglucan oligosaccharides is vital for IpeA activity. We solved the crystal structure of IpeA with isoprimeverose at 2.4 Å resolution, showing that the structure of IpeA formed a dimer and was composed of three domains: an N-terminal (β/α) TIM-barrel domain, α/β/α sandwich fold domain, and a C-terminal fibronectin-like domain. The catalytic TIM-barrel domain possessed a catalytic nucleophile (Asp300) and acid/base (Glu524) residues. Interestingly, we found that the cavity of the active site of IpeA was larger than that of other GH3 enzymes, and subsite -1' played an important role in its activity. The glucopyranosyl and xylopyranosyl residues of isoprimeverose were located at subsites -1 and -1', respectively. Gln58 and Tyr89 contributed to the interaction with the xylopyranosyl residue of isoprimeverose through hydrogen bonding and stacking effects, respectively. Our findings provide new insights into the substrate recognition of GH3 enzymes.

PubMed: 30445155
DOI: 10.1016/j.jsb.2018.11.005

実験手法

X-RAY DIFFRACTION (2.4 Å)