Evolution of structural dynamics in proteins

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Proteins are essential building blocks of life that conduct numerous biological functions by use of specific three-dimensional folds and structural dynamics. While the evolutionary development of protein function has become well characterized, the details of how structural dynamics emerged evolutionary remains unclear. How does nature utilize structural dynamics to diversify function?

To shed light on this, a team led by LMU biophysicist Thorben Cordes and structural biologist Giorgos Gouridis from the IMBB FORTH in Crete (Greece) analysed bilobed proteins with a common structural core. This core is widely spread throughout the tree of life and is involved in diverse biological functions such as transcription, enzymatic catalysis, membrane transport and signalling. The scientists show that the structural dynamics of the core differentiate predominantly via terminal additions during a long-period evolution. This allows to diversify substrate specificity, ligand binding mechanisms and ultimately biological function.

Giorgos Gouridis, Yusran A. Muthahari, Marijn de Boer, Douglas A. Griffith, Alexandra Tsirigotaki, Konstantinos Tassis, Niels Zijlstra, Ruixue Xu, Nikolaos Eleftheriadis, Yovin Sugijo, Martin Zacharias, Alexander Dömling, Spyridoula Karamanou, Charalambos Pozidis, Anastassios Economou and Thorben Cordes: Structural dynamics in the evolution of a bilobed protein scaffold. PNAS 2021