3VGI

The crystal structure of hyperthermophilic family 12 endocellulase from Pyrococcus furiosus

3VGI の概要

• エントリーDOI: 10.2210/pdb3vgi/pdb
• 関連するPDBエントリー: 3AZ0
• 分子名称: Endoglucanase A, CALCIUM ION, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, ... (5 entities in total)
• 機能のキーワード: beta-jelly roll fold, hydrolase, carbohydrate/sugar binding
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37483.27

構造登録者

Kataoka, M.,Kim, H.-W.,Ishikawa, K. (登録日: 2011-08-11, 公開日: 2012-09-12, 最終更新日: 2024-03-20)

主引用文献

Kim, H.-W.,Kataoka, M.,Ishikawa, K.
Atomic resolution of the crystal structure of the hyperthermophilic family 12 endocellulase and stabilizing role of the DxDxDG calcium-binding motif in Pyrococcus furiosus.
Febs Lett., 586:1009-1013, 2012

PubMed Abstract: Hyperthermophilic glycoside hydrolase family 12 endocellulase (EGPf) from the archaeon Pyrococcus furiosus catalyzes the hydrolytic cleavage of β-1,4-glucosidic linkage in β-glucan cellulose. A truncated EGPf (EGPfΔN30) mutant lacking the proline and hydroxyl-residue rich region at the N terminus was constructed, and its crystal structure was resolved at an atomic resolution of 1.07 Å. Our results indicate that the structure of EGPf, which consists of a β-jelly roll, exhibits structural similarity with the endocellulase of Thermotoga maritima. Additionally, we further determined that the thermostability of EGPf is maintained in part by the binding of Ca²⁺ in a DxDxDG Ca²⁺-binding motif, atypical of most archaeal proteins.

PubMed: 22569255
DOI: 10.1016/j.febslet.2012.02.029

実験手法

X-RAY DIFFRACTION (1.07 Å)