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J. Biol. Chem., Vol. 283, Issue 45, 31142-31152, November 7, 2008
An Unusual Intrinsically Disordered Protein from the Model Legume Lotus japonicus Stabilizes Proteins in Vitro* 1 2![]() 4
From the
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 β-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
Received for publication, July 2, 2008 , and in revised form, September 5, 2008. * The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. 1 Supported by the Danish Biotech Research Academy (DBRA) and the Danish National Research Foundation (Research Centre CARB). 2 Supported by the Danish National Research Foundation (Research Centre CARB). 3 Supported by the Danish Research Science Foundation (Research Centre inSPIN) and the Villum Kann Rasmussen Foundation (Research Centre BioNET). 4 Supported by the Danish National Research Foundation (Research Centre CARB). To whom correspondence should be addressed: Gustav Wieds Vej 10, Aarhus 8000, Denmark. Fax: 45-86123178; E-mail: stougaard{at}mb.au.dk.
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