4G4I

Crystal structure of glucuronoyl esterase S213A mutant from Sporotrichum thermophile determined at 1.9 A resolution

4G4I の概要

• エントリーDOI: 10.2210/pdb4g4i/pdb
• 関連するPDBエントリー: 4G4G 4G4J
• 分子名称: 4-O-methyl-glucuronoyl methylesterase, 1,2-ETHANEDIOL, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: alpha/beta hydrolase, 3-layer alpha/beta/alpha sandwich, rossmann fold, glucuronoyl esterase, hydrolase
• 由来する生物種: Myceliophthora thermophila
• 細胞内の位置: Secreted : G2QJR6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46818.99

構造登録者

Charvagi, M.D.,Dimarogona, M.,Topakas, E.,Christakopoulos, P.,Chrysina, E.D. (登録日: 2012-07-16, 公開日: 2013-01-02, 最終更新日: 2024-11-06)

主引用文献

Charavgi, M.D.,Dimarogona, M.,Topakas, E.,Christakopoulos, P.,Chrysina, E.D.
The structure of a novel glucuronoyl esterase from Myceliophthora thermophila gives new insights into its role as a potential biocatalyst.
Acta Crystallogr.,Sect.D, 69:63-73, 2013

PubMed Abstract: The increasing demand for the development of efficient biocatalysts is a consequence of their broad industrial applications. Typical difficulties that are encountered during their exploitation in a variety of processes are interconnected with factors such as temperature, pH, product inhibitors etc. To eliminate these, research has been directed towards the identification of new enzymes that would comply with the required standards. To this end, the recently discovered glucuronoyl esterases (GEs) are an enigmatic family within the carbohydrate esterase (CE) family. Structures of the thermophilic StGE2 esterase from Myceliophthora thermophila (synonym Sporotrichum thermophile), a member of the CE15 family, and its S213A mutant were determined at 1.55 and 1.9 Å resolution, respectively. The first crystal structure of the S213A mutant in complex with a substrate analogue, methyl 4-O-methyl-β-D-glucopyranuronate, was determined at 2.35 Å resolution. All of the three-dimensional protein structures have an α/β-hydrolase fold with a three-layer αβα-sandwich architecture and a Rossmann topology and comprise one molecule per asymmetric unit. These are the first crystal structures of a thermophilic GE both in an unliganded form and bound to a substrate analogue, thus unravelling the organization of the catalytic triad residues and their neighbours lining the active site. The knowledge derived offers novel insights into the key structural elements that drive the hydrolysis of glucuronic acid esters.

PubMed: 23275164
DOI: 10.1107/S0907444912042400

実験手法

X-RAY DIFFRACTION (1.9 Å)