5B6S

Catalytic domain of Coprinopsis cinerea GH62 alpha-L-arabinofuranosidase

5B6S の概要

• エントリーDOI: 10.2210/pdb5b6s/pdb
• 関連するPDBエントリー: 5B6T
• 分子名称: Glycosyl hydrolase family 62 protein, CALCIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: coprinopsis cinerea, alpha-l-arabinofuranosidase, arabinoxylan, gh62, hemicellulose, hydrolase
• 由来する生物種: Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) (Inky cap fungus)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74005.45

構造登録者

Tonozuka, T. (登録日: 2016-06-01, 公開日: 2016-09-07, 最終更新日: 2024-11-20)

主引用文献

Tonozuka, T.,Tanaka, Y.,Okuyama, S.,Miyazaki, T.,Nishikawa, A.,Yoshida, M.
Structure of the Catalytic Domain of alpha-L-Arabinofuranosidase from Coprinopsis cinerea, CcAbf62A, Provides Insights into Structure-Function Relationships in Glycoside Hydrolase Family 62
Appl. Biochem. Biotechnol., 181:511-525, 2017

PubMed Abstract: α-L-Arabinofuranosidases, belonging to the glycoside hydrolase family (GH) 62, hydrolyze the α-1,2- or α-1,3-bond to liberate L-arabinofuranose from the xylan backbone. Here, we determined the structure of the C-terminal catalytic domain of CcAbf62A, a GH62 α-L-arabinofuranosidase from Coprinopsis cinerea. CcAbf62A is composed of a five-bladed β-propeller, as observed in other GH62 enzymes. The structure near the active site of CcAbf62A is also highly homologous to those of other GH62 enzymes. However, a calcium atom in the catalytic center interacts with an asparagine residue, Asn279, which is not found in other GH62 enzymes. In addition, some residues in subsites +3R, +2NR, +3NR, and +4NR of CcAbf62A are not conserved in other GH62 enzymes. In particular, a histidine residue, His221, is uniquely observed in subsite +2NR of CcAbf62A, which is likely to influence the substrate specificity. The results obtained here suggest that the amino acid residues that interact with the xylan backbone vary among the GH62 enzymes, despite the high similarity of their overall structures.

PubMed: 27589854
DOI: 10.1007/s12010-016-2227-0

実験手法

X-RAY DIFFRACTION (1.7 Å)