2VY0

The X-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus

2VY0 の概要

• エントリーDOI: 10.2210/pdb2vy0/pdb
• 分子名称: ENDO-BETA-1,3-GLUCANASE, CHLORIDE ION, SODIUM ION, ... (7 entities in total)
• 機能のキーワード: hydrolase, laminarin, endoglucanase, thermostable protein
• 由来する生物種: PYROCOCCUS FURIOSUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61016.06

構造登録者

Ilari, A.,Fiorillo, A. (登録日: 2008-07-15, 公開日: 2009-03-24, 最終更新日: 2023-12-13)

主引用文献

Ilari, A.,Fiorillo, A.,Angelaccio, S.,Florio, R.,Chiaraluce, R.,Van Der Oost, J.,Consalvi, V.
Crystal Structure of a Family 16 Endoglucanase from the Hyperthermophile Pyrococcus Furiosus-Structural Basis of Substrate Recognition.
FEBS J., 276:1048-, 2009

PubMed Abstract: Bacterial and archaeal endo-beta-1,3-glucanases that belong to glycoside hydrolase family 16 share a beta-jelly-roll fold, but differ significantly in sequence and in substrate specificity. The crystal structure of the laminarinase (EC 3.2.1.39) from the hyperthermophilic archaeon Pyrococcus furiosus (pfLamA) has been determined at 2.1 A resolution by molecular replacement. The pfLamA structure reveals a kink of six residues (72-77) at the entrance of the catalytic cleft. This peptide is absent in the endoglucanases from alkaliphilic Nocardiopsis sp. strain F96 and Bacillus macerans, two proteins displaying an overall fold similar to that of pfLamA, but with different substrate specificity. A deletion mutant of pfLamA, lacking residues 72-75, hydrolyses the mixed-linkage beta-1,3-1,4-glucan lichenan 10 times more efficiently than the wild-type protein, indicating the importance of the kink in substrate preference.

PubMed: 19154353
DOI: 10.1111/J.1742-4658.2008.06848.X

実験手法

X-RAY DIFFRACTION (2.16 Å)