2K7J

Human Acylphosphatase(AcPh) surface charge-optimized

2K7J の概要

• エントリーDOI: 10.2210/pdb2k7j/pdb
• 関連するPDBエントリー: 2K7K
• 分子名称: Acylphosphatase-1 (1 entity in total)
• 機能のキーワード: protein, acetylation, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11210.79

構造登録者

Gribenko, A.V.,Patel, M.M.,Liu, J.,McCallum, S.A.,Wang, C.,Makhatadze, G.I. (登録日: 2008-08-12, 公開日: 2009-02-17, 最終更新日: 2024-05-22)

主引用文献

Gribenko, A.V.,Patel, M.M.,Liu, J.,McCallum, S.A.,Wang, C.,Makhatadze, G.I.
Rational stabilization of enzymes by computational redesign of surface charge-charge interactions
Proc.Natl.Acad.Sci.USA, 106:2601-2606, 2009

PubMed Abstract: Here, we report the application of a computational approach that allows the rational design of enzymes with enhanced thermostability while retaining full enzymatic activity. The approach is based on the optimization of the energy of charge-charge interactions on the protein surface. We experimentally tested the validity of the approach on 2 human enzymes, acylphosphatase (AcPh) and Cdc42 GTPase, that differ in size (98 vs. 198-aa residues, respectively) and tertiary structure. We show that the designed proteins are significantly more stable than the corresponding WT proteins. The increase in stability is not accompanied by significant changes in structure, oligomerization state, or, most importantly, activity of the designed AcPh or Cdc42. This success of the design methodology suggests that it can be universally applied to other enzymes, on its own or in combination with the other strategies based on redesign of the interactions in the protein core.

PubMed: 19196981
DOI: 10.1073/pnas.0808220106

実験手法

SOLUTION NMR