4CNW

Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture

4CNW の概要

• エントリーDOI: 10.2210/pdb4cnw/pdb
• 関連するPDBエントリー: 4CNR 4CNV 4CNX
• 分子名称: CARBONIC ANHYDRASE 2, ZINC ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: lyase, protein engineering, co2 capture
• 由来する生物種: BOS TAURUS (CATTLE)
• 細胞内の位置: Cytoplasm: P00921
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58960.03

構造登録者

Warden, A.,Newman, J.,Peat, T.S.,Seabrook, S.,Williams, M.,Dojchinov, G.,Haritos, V. (登録日: 2014-01-25, 公開日: 2015-02-04, 最終更新日: 2023-12-20)

主引用文献

Warden, A.C.,Williams, M.,Peat, T.S.,Seabrook, S.A.,Newman, J.,Dojchinov, G.,Haritos, V.S.
Rational Engineering of a Mesohalophilic Carbonic Anhydrase to an Extreme Halotolerant Biocatalyst.
Nat.Commun., 6:10278-, 2015

PubMed Abstract: Enzymes expressed by highly salt-tolerant organisms show many modifications compared with salt-affected counterparts including biased amino acid and lower α-helix content, lower solvent accessibility and negative surface charge. Here, we show that halotolerance can be generated in an enzyme solely by modifying surface residues. Rational design of carbonic anhydrase II is undertaken in three stages replacing 18 residues in total, crystal structures confirm changes are confined to surface residues. Catalytic activities and thermal unfolding temperatures of the designed enzymes increase at high salt concentrations demonstrating their shift to halotolerance, whereas the opposite response is found in the wild-type enzyme. Molecular dynamics calculations reveal a key role for sodium ions in increasing halotolerant enzyme stability largely through interactions with the highly ordered first Na(+) hydration shell. For the first time, an approach to generate extreme halotolerance, a trait with broad application in industrial biocatalysis, in a wild-type enzyme is demonstrated.

PubMed: 26687908
DOI: 10.1038/NCOMMS10278

実験手法

X-RAY DIFFRACTION (2.03 Å)