Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.

ABSTRACT: Bacteria exploit surface proteins to adhere to other bacteria, surfaces and host cells. Such proteins need to project away from the bacterial surface and resist significant mechanical forces. SasG is a protein that forms extended fibrils on the surface of Staphylococcus aureus and promotes host adherence and biofilm formation. Here we show that although monomeric and lacking covalent cross-links, SasG maintains a highly extended conformation in solution. This extension is mediated through obligate folding cooperativity of the intrinsically disordered E domains that couple non-adjacent G5 domains thermodynamically, forming interfaces that are more stable than the domains themselves. Thus, counterintuitively, the elongation of the protein appears to be dependent on the inherent instability o

SUBMITTER: Gruszka DT 

PROVIDER: S-EPMC4458895 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature