Decoding the intricate network of molecular interactions of a hyperstable engineered biocatalyst.

ABSTRACT: Computational design of protein catalysts with enhanced stabilities for use in research and enzyme technologies is a challenging task. Using force-field calculations and phylogenetic analysis, we previously designed the haloalkane dehalogenase DhaA115 which contains 11 mutations that confer upon it outstanding thermostability (T _m = 73.5 °C; ΔT _m > 23 °C). An understanding of the structural basis of this hyperstabilization is required in order to develop computer algorithms and predictive tools. Here, we report X-ray structures of DhaA115 at 1.55 Å and 1.6 Å resolutions and their molecular dynamics trajectories, which unravel the intricate network of interactions that reinforce the αβα-sandwich architecture. Unexpectedly, mutations toward bulky aromatic

SUBMITTER: Markova K 

PROVIDER: S-EPMC8162949 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature