3PBJ

Hydrolytic catalysis and structural stabilization in a designed metalloprotein

3PBJ の概要

• エントリーDOI: 10.2210/pdb3pbj/pdb
• 関連するPDBエントリー: 2JGO 2X6P 3H5F 3H5G 3LJM
• 分子名称: COIL SER L9L-Pen L23H, ZINC ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: de novo protein, parallel three-stranded coiled coil, mercury(ii) binding protein, zinc(ii) binding protein, l-penicillamine
• 由来する生物種: artificial gene
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 21261.74

構造登録者

Zastrow, M.L.,Peacock, A.F.A.,Stuckey, J.A.,Pecoraro, V.L. (登録日: 2010-10-20, 公開日: 2011-11-30, 最終更新日: 2022-05-04)

主引用文献

Zastrow, M.L.,Peacock, A.F.,Stuckey, J.A.,Pecoraro, V.L.
Hydrolytic catalysis and structural stabilization in a designed metalloprotein.
Nat Chem, 4:118-123, 2012

PubMed Abstract: Metal ions are an important part of many natural proteins, providing structural, catalytic and electron transfer functions. Reproducing these functions in a designed protein is the ultimate challenge to our understanding of them. Here, we present an artificial metallohydrolase, which has been shown by X-ray crystallography to contain two different metal ions-a Zn(II) ion, which is important for catalytic activity, and a Hg(II) ion, which provides structural stability. This metallohydrolase displays catalytic activity that compares well with several characteristic reactions of natural enzymes. It catalyses p-nitrophenyl acetate (pNPA) hydrolysis with an efficiency only ~100-fold less than that of human carbonic anhydrase (CA)II and at least 550-fold better than comparable synthetic complexes. Similarly, CO(2) hydration occurs with an efficiency within ~500-fold of CAII. Although histidine residues in the absence of Zn(II) exhibit pNPA hydrolysis, miniscule apopeptide activity is observed for CO(2) hydration. The kinetic and structural analysis of this first de novo designed hydrolytic metalloenzyme reveals necessary design features for future metalloenzymes containing one or more metals.

PubMed: 22270627
DOI: 10.1038/nchem.1201

実験手法

X-RAY DIFFRACTION (2.2 Å)