3WID

Structure of a glucose dehydrogenase T277F mutant in complex with NADP

3WID の概要

• エントリーDOI: 10.2210/pdb3wid/pdb
• 関連するPDBエントリー: 3wic 3wie
• 分子名称: Glucose 1-dehydrogenase, ZINC ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total)
• 機能のキーワード: rossmann fold, oxidoreductase
• 由来する生物種: Thermoplasma volcanium
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 171102.31

構造登録者

Sakuraba, H.,Kanoh, Y.,Yoneda, K.,Ohshima, T. (登録日: 2013-09-10, 公開日: 2014-05-14, 最終更新日: 2023-11-08)

主引用文献

Kanoh, Y.,Uehara, S.,Iwata, H.,Yoneda, K.,Ohshima, T.,Sakuraba, H.
Structural insight into glucose dehydrogenase from the thermoacidophilic archaeon Thermoplasma volcanium.
Acta Crystallogr.,Sect.D, 70:1271-1280, 2014

PubMed Abstract: Glucose dehydrogenase from the thermoacidophilic archaeon Thermoplasma volcanium (tvGlcDH) is highly active towards D-glucose and D-galactose, but does not utilize aldopentoses such as D-xylose as substrates. In the present study, the crystal structures of substrate/cofactor-free tvGlcDH and of a tvGlcDH T277F mutant in a binary complex with NADP and in a ternary complex with D-glucose and nicotinic acid adenine dinucleotide phosphate, an NADP analogue, were determined at resolutions of 2.6, 2.25 and 2.33 Å, respectively. The overall structure of each monomer showed notable similarity to that of the enzyme from Sulfolobus solfataricus (ssGlcDH-1), which accepts a broad range of C5 and C6 sugars as substrates. However, the amino-acid residues of tvGlcDH involved in substrate binding markedly differed from those of ssGlcDH-1. Structural comparison revealed that a decreased number of interactions between the C3-hydroxyl group of the sugar and the enzyme are likely to be responsible for the lack of reactivity of tvGlcDH towards D-xylose.

PubMed: 24816096
DOI: 10.1107/S1399004714002363

実験手法

X-RAY DIFFRACTION (2.25 Å)