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Title 

Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity

Authors 

Seung Jun KimDae Gwin JeongSeung Wook ChiJin Sook LeeSeong Eon Ryu

Publisher 

Nature Publishing Group

Issue Date 

2001

Citation 

Nature Structural Biology, vol. 8, no. 5, pp. 459-466

Keywords 

chaperonecrystal structurecrystallography, X-Raymolecular chaperonespeptide fragmentsprotein structure, quaternaryprotein structure, tertiary

Abstract 

Heat shock protein 33 (Hsp33) inhibits aggregation of partially denatured proteins during oxidative stress. The chaperone activity of Hsp33 is unique among heat shock proteins because the activity is reversibly regulated by cellular redox status. We report here the crystal structure of the N-terminal region of Hsp33 fragments with constitutive chaperone activity. The structure reveals that the N-terminal portion of Hsp33 forms a tightly associated dimer formed by a domain crossover. A concave groove on the dimeric surface contains an elongated hydrophobic patch that could potentially bind denatured protein substrates. The termini of the subunits are located near the hydrophobic patch, indicating that the cleaved C-terminal domain may shield the hydrophobic patch in an inactive state. Two of the four conserved zinc-coordinating cysteines are in the end of the N-terminal domain, and the other two are in the cleaved C-terminal domain. The structural information and subsequent biochemical characterizations suggest that the redox switch of Hsp33 occurrs by a reversible dissociation of the C-terminal regulatory domain through oxidation of zinc-coordinating cysteines and zinc release.

ISSN 

1072-8368

Link 

http://dx.doi.org/10.1038/87639

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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