Open AccessStructural dynamics in the evolution of a bilobed protein scaffold
Author(s) -
Giorgos Gouridis,
Yusran Abdillah Muthahari,
Marijn de Boer,
Douglas A. Griffith,
Alexandra Tsirigotaki,
Konstantinos Tassis,
Niels Zijlstra,
Rui-Xue Xu,
Nikolaos Eleftheriadis,
Yovin Sugijo,
Martin Zacharias,
Alexander Dömlingꝉ,
Spyridoula Karamanou,
Charalambos Pozidis,
Anastassios Economou,
Thorben Cordes
Publication year - 2021
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2026165118
Subject(s) - protein dynamics , structural similarity , structural biology , periplasmic space , protein structure , biology , computational biology , biophysics , structural motif , molecular dynamics , protein domain , förster resonance energy transfer , chemistry , evolutionary biology , microbiology and biotechnology , genetics , biochemistry , physics , gene , computational chemistry , escherichia coli , quantum mechanics , fluorescence
Significance Proteins conduct numerous complex biological functions by use of tailored structural dynamics. The molecular details of how these emerged from ancestral peptides remains mysterious. How does nature utilize the same repertoire of folds to diversify function? To shed light on this, we analyzed bilobed proteins with a common structural core, which is spread throughout the tree of life and is involved in diverse biological functions such as transcription, enzymatic catalysis, membrane transport, and signaling. We show here that the structural dynamics of the structural core differentiate predominantly via terminal additions during a long-period evolution. This diversifies substrate specificity and, ultimately, biological function.