Open AccessDesign structure of fusion protein of bovine DNA exotransferase and E. coli SSB protein
Author(s) -
A. B. Sachanka,
Ya. U. Dzichenka,
A. V. Yantsevich,
Sergey A. Usanov
Publication year - 2021
Publication title -
doklady nacionalʹnoj akademii nauk belarusi
Language(s) - English
Resource type - Journals
eISSN - 2524-2431
pISSN - 1561-8323
DOI - 10.29235/1561-8323-2021-65-5-568-575
Subject(s) - fusion protein , dna , structural similarity , chemistry , enzyme , fusion , dna binding domain , escherichia coli , biochemistry , biology , biophysics , microbiology and biotechnology , recombinant dna , gene , linguistics , philosophy , transcription factor
The analysis of the trajectories of molecular dynamics simulation and spatial structures of homologous models of fusion protein with various linkers was performed to understand the effect of the additional DNA-binding domain of the E. coli SSB protein attached to the truncated and native bovine DNA exotransferase on its stability and activity. It is found that the C-terminus of the enzyme is the preferred end for attachment of the E. coli protein, while the stability of the truncated fusion enzyme is higher than the native one. According to molecular dynamics data, introducing linkers between two proteins for the native (GGGGSGGGSGGGGS, GGGSGGGS, and TCT) and truncated (GGSGGGSGG, , GTGSGT, and 5xGGGGS) forms of the enzyme not only improves its stability, but also increases the mutual mobility of DNA-affinity domains.