Shared dynamics of LeuT superfamily members and allosteric differentiation by structural irregularities and multimerization.

ABSTRACT: The LeuT-fold superfamily includes secondary active transporters from different functional families, which share a common tertiary structure, despite having a remarkably low sequence similarity. By identifying the common structural and dynamical features upon principal component analysis of a comprehensive ensemble of 90 experimentally resolved structures and anisotropic network model evaluation of collective motions, we provide a unified point of view for understanding the reasons why this particular fold has been selected by evolution to accomplish such a broad spectrum of functions. The parallel identification of conserved sequence features, localized at specific sites of transmembrane helices, sheds light on the role of broken helices (TM1 and TM6 in LeuT) in promoting ion/substrate bi

SUBMITTER: Ponzoni L 

PROVIDER: S-EPMC5941172 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature