8JA4

Structure of the alginate epimerase/lyase

これはPDB形式変換不可エントリーです。

8JA4 の概要

• エントリーDOI: 10.2210/pdb8ja4/pdb
• 分子名称: mannuronan 5-epimerase, CALCIUM ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: bifunctional epimerase/lyase, isomerase
• 由来する生物種: Azotobacter chroococcum NCIMB 8003
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53543.58

構造登録者

Fujiwara, T. (登録日: 2023-05-05, 公開日: 2024-05-08, 最終更新日: 2024-06-26)

主引用文献

Fujiwara, T.,Mano, E.,Nango, E.
Structural basis for the minimal bifunctional alginate epimerase AlgE3 from Azotobacter chroococcum.
Febs Lett., 598:1422-1437, 2024

PubMed Abstract: Among the epimerases specific to alginate, some of them in Azotobacter genera convert β-d-mannuronic acid to α-l-guluronic acid but also have lyase activity to degrade alginate. The remarkable characteristics of these epimerases make it a promising enzyme for tailoring alginates to meet specific demands. Here, we determined the structure of the bifunctional mannuronan C-5 epimerase AlgE3 from Azotobacter chroococcum (AcAlgE3) in complex with several mannuronic acid oligomers as well as in apo form, which allowed us to elucidate the binding manner of each mannuronic acid oligomer, and the structural plasticity, which is dependent on calcium ions. Moreover, a comprehensive analysis of the lyase activity profiles of AcAlgE3 combined with structural characteristics explained the preference for different chain length oligomers.

PubMed: 38649293
DOI: 10.1002/1873-3468.14886

実験手法

X-RAY DIFFRACTION (2.04 Å)