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  • Title: Subunit arrangement in the dodecameric chloroplast small heat shock protein Hsp21.
    Author: Lambert W, Koeck PJ, Ahrman E, Purhonen P, Cheng K, Elmlund D, Hebert H, Emanuelsson C.
    Journal: Protein Sci; 2011 Feb; 20(2):291-301. PubMed ID: 21280121.
    Abstract:
    Unfolding proteins are prevented from irreversible aggregation by small heat shock proteins (sHsps) through interactions that depend on a dynamic equilibrium between sHsp subunits and sHsp oligomers. A chloroplast-localized sHsp, Hsp21, provides protection to client proteins to increase plant stress resistance. Structural information is lacking concerning the oligomeric conformation of this sHsp. We here present a structure model of Arabidopsis thaliana Hsp21, obtained by homology modeling, single-particle electron microscopy, and lysine-specific chemical crosslinking. The model shows that the Hsp21 subunits are arranged in two hexameric discs, similar to a cytosolic plant sHsp homolog that has been structurally determined after crystallization. However, the two hexameric discs of Hsp21 are rotated by 25° in relation to each other, suggesting a role for global dynamics in dodecamer function.
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