Conserved energetic changes drive function in an ancient protein fold.

ABSTRACT: Many protein sequences occupy similar three-dimensional structures known as protein folds. In nature, protein folds are well-conserved over the course of evolution, such that there are 100,000 times as many extant protein sequences than there are folds. Despite their common shapes, similar protein folds can adopt wide-ranging functions, raising the question: are protein folds so strongly conserved for the purpose of maintaining function-driving energetic changes in protein families? Here we show that a set of key energetic relationships in a family of bacterial transcription factors (TFs) is conserved using high-resolution hydrogen exchange/mass spectrometry, bioinformatics, X-ray crystallography, and molecular dynamics simulations. We compared the TFs to their anciently diverged structura

SUBMITTER: Wells ML 

PROVIDER: S-EPMC12026503 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature