Influence of circular permutations on the structure and stability of a six-fold circular symmetric designer protein.

ABSTRACT: The β-propeller fold is adopted by a sequentially diverse family of repeat proteins with apparent rotational symmetry. While the structure is mostly stabilized by hydrophobic interactions, an additional stabilization is provided by hydrogen bonds between the N-and C-termini, which are almost invariably part of the same β-sheet. This feature is often referred to as the "Velcro" closure. The positioning of the termini within a blade is variable and depends on the protein family. In order to investigate the influence of this location on protein structure, folding and stability, we created different circular permutants, and a circularized version, of the designer propeller protein named Pizza. This protein is perfectly symmetrical, possessing six identical repeats. While all mutants adopt the

SUBMITTER: Mylemans B 

PROVIDER: S-EPMC7679965 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature