Structural and mutational analyses of psychrophilic and mesophilic adenylate kinases highlight the role of hydrophobic interactions in protein thermal stability
作者： Sojin Moon , Junhyung Kim , Jasung Koo , Euiyoung Bae
DOI: 10.1063/1.5089707
关键词:
摘要: Protein thermal stability is an important field since thermally stable proteins are desirable in many academic and industrial settings. Information on protein stabilization can be obtained by comparing homologous from organisms living at distinct temperatures. Here, we report structural mutational analyses of adenylate kinases (AKs) psychrophilic Bacillus globisporus (AKp) mesophilic subtilis (AKm). Sequence comparison showed suboptimal hydrophobic packing around Thr26 the CORE domain AKp, which was replaced with Ile residue AKm. Mutations that improved hydrophobicity Thr increased largest observed for a Thr-to-Ile substitution. Furthermore, reverse Ile-to-Thr mutation AKm significantly decreased stability. We determined crystal structures mutant AKs to confirm impact substitutions overall Taken together, our results provide basis difference between AK homologues highlight role interactions
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