An unusual intrinsically disordered protein from the model legume Lotus japonicus stabilizes proteins in vitro.

ABSTRACT: Intrinsic structural disorder is a prevalent feature of proteins with chaperone activity. Using a complementary set of techniques, we have structurally characterized LjIDP1 (intrinsically disordered protein 1) from the model legume Lotus japonicus, and our results provide the first structural characterization of a member of the Lea5 protein family (PF03242). Contrary to in silico predictions, we show that LjIDP1 is intrinsically disordered and probably exists as an ensemble of conformations with limited residual beta-sheet, turn/loop, and polyproline II secondary structure. Furthermore, we show that LjIDP1 has an inherent propensity to undergo a large conformational shift, adopting a largely alpha-helical structure when it is dehydrated and in the presence of different detergents and alcoh

SUBMITTER: Haaning S 

PROVIDER: S-EPMC2662180 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature