3A9G

Crystal Structure of PQQ-dependent sugar dehydrogenase apo-form

3A9G の概要

• エントリーDOI: 10.2210/pdb3a9g/pdb
• 関連するPDBエントリー: 3A9H
• 関連するBIRD辞書のPRD_ID: PRD_900006
• 分子名称: Putative uncharacterized protein, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: pqq dependent dehydrogenase, aldose sugar dehydrogenase, beta-propeller fold, oxidoreductase
• 由来する生物種: Pyrobaculum aerophilum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39096.28

構造登録者

Sakuraba, H.,Yokono, K.,Yoneda, K.,Ohshima, T. (登録日: 2009-10-26, 公開日: 2010-09-08, 最終更新日: 2023-11-01)

主引用文献

Sakuraba, H.,Yokono, K.,Yoneda, K.,Watanabe, A.,Asada, Y.,Satomura, T.,Yabutani, T.,Motonaka, J.,Ohshima, T.
Catalytic properties and crystal structure of quinoprotein aldose sugar dehydrogenase from hyperthermophilic archaeon Pyrobaculum aerophilum
Arch.Biochem.Biophys., 502:81-88, 2010

PubMed Abstract: We identified a gene encoding a soluble quinoprotein glucose dehydrogenase homologue in the hyperthermophilic archaeon Pyrobaculum aerophilum. The gene was overexpressed in Escherichia coli, after which its product was purified and characterized. The enzyme was extremely thermostable, and the activity of the pyrroloquinoline quinone (PQQ)-bound holoenzyme was not lost after incubation at 100 degrees C for 10 min. The crystal structure of the enzyme was determined in both the apoform and as the PQQ-bound holoenzyme. The overall fold of the P. aerophilum enzyme showed significant similarity to that of soluble quinoprotein aldose sugar dehydrogenase (Asd) from E. coli. However, clear topological differences were observed in the two long loops around the PQQ-binding sites of the two enzymes. Structural comparison revealed that the hyperthermostability of the P. aerophilum enzyme is likely attributable to the presence of an extensive aromatic pair network located around a beta-sheet involving N- and C-terminal beta-strands.

PubMed: 20692227
DOI: 10.1016/j.abb.2010.08.002

実験手法

X-RAY DIFFRACTION (2.39 Å)