1I7F

CRYSTAL STRUCTURE OF THE HSP33 DOMAIN WITH CONSTITUTIVE CHAPERONE ACTIVITY

Summary for 1I7F

• Entry DOI: 10.2210/pdb1i7f/pdb
• Descriptor: HEAT SHOCK PROTEIN 33, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: hsp33, redox sensitive molecular chaperone, chaperone
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 33169.72

Authors

Kim, S.-J.,Jeong, D.-G.,Chi, S.-W.,Lee, J.-S.,Ryu, S.-E. (deposition date: 2001-03-09, release date: 2001-05-09, Last modification date: 2024-10-09)

Primary citation

Kim, S.J.,Jeong, D.G.,Chi, S.W.,Lee, J.S.,Ryu, S.E.
Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity
Nat.Struct.Biol., 8:459-466, 2001

PubMed 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 occurs by a reversible dissociation of the C-terminal regulatory domain through oxidation of zinc-coordinating cysteines and zinc release.

PubMed: 11323724
DOI: 10.1038/87603

Experimental method

X-RAY DIFFRACTION (2.7 Å)