4U9D

Crystal Structure of the Zn-directed tetramer of the engineered cyt cb562 variant, AB3

4U9D の概要

• エントリーDOI: 10.2210/pdb4u9d/pdb
• 分子名称: Soluble cytochrome b562, HEME C, ZINC ION, ... (4 entities in total)
• 機能のキーワード: designed enzyme, zn-coordinating protein, tetramer assembly, metal binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 50338.33

構造登録者

Tezcan, F.A.,Song, W.J. (登録日: 2014-08-05, 公開日: 2015-01-14, 最終更新日: 2023-12-27)

主引用文献

Song, W.J.,Tezcan, F.A.
A designed supramolecular protein assembly with in vivo enzymatic activity.
Science, 346:1525-1528, 2014

PubMed Abstract: The generation of new enzymatic activities has mainly relied on repurposing the interiors of preexisting protein folds because of the challenge in designing functional, three-dimensional protein structures from first principles. Here we report an artificial metallo-β-lactamase, constructed via the self-assembly of a structurally and functionally unrelated, monomeric redox protein into a tetrameric assembly that possesses catalytic zinc sites in its interfaces. The designed metallo-β-lactamase is functional in the Escherichia coli periplasm and enables the bacteria to survive treatment with ampicillin. In vivo screening of libraries has yielded a variant that displays a catalytic proficiency [(k(cat)/K(m))/k(uncat)] for ampicillin hydrolysis of 2.3 × 10(6) and features the emergence of a highly mobile loop near the active site, a key component of natural β-lactamases to enable substrate interactions.

PubMed: 25525249
DOI: 10.1126/science.1259680

実験手法

X-RAY DIFFRACTION (2.5 Å)