7FDY

Structure of OmpF1

7FDY の概要

• エントリーDOI: 10.2210/pdb7fdy/pdb
• 分子名称: Porin OmpF, ZINC ION (3 entities in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 111743.20

構造登録者

Jeong, W.J.,Song, W.J. (登録日: 2021-07-18, 公開日: 2022-11-16, 最終更新日: 2023-11-29)

主引用文献

Jeong, W.J.,Song, W.J.
Design and directed evolution of noncanonical beta-stereoselective metalloglycosidases.
Nat Commun, 13:6844-6844, 2022

PubMed Abstract: Metallohydrolases are ubiquitous in nearly all subclasses of hydrolases, utilizing metal elements to activate a water molecule and facilitate its subsequent dissociation of diverse chemical bonds. However, such a catalytic role of metal ions is rarely found with glycosidases that hydrolyze the glycosidic bonds in sugars. Herein, we design metalloglycosidases by constructing a hydrolytically active Zn-binding site within a barrel-shaped outer membrane protein OmpF. Structure- and mechanism-based redesign and directed evolution have led to the emergence of Zn-dependent glycosidases with catalytic proficiency of 2.8 × 10 and high β-stereoselectivity. Biochemical characterizations suggest that the Zn-binding site constitutes a key catalytic motif along with at least one adjacent acidic residue. This work demonstrates that unprecedented metalloenzymes can be tailor-made, expanding the scope of inorganic reactivities in proteinaceous environments, resetting the structural and functional diversity of metalloenzymes, and providing the potential molecular basis of unidentified metallohydrolases and novel whole-cell biocatalysts.

PubMed: 36369431
DOI: 10.1038/s41467-022-34713-8

実験手法

X-RAY DIFFRACTION (3.1 Å)