1HW7

HSP33, HEAT SHOCK PROTEIN WITH REDOX-REGULATED CHAPERONE ACTIVITY

Summary for 1HW7

• Entry DOI: 10.2210/pdb1hw7/pdb
• Descriptor: HEAT SHOCK PROTEIN HSP33, SULFATE ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: hsp33, dimerization, heat shock protein, oxidative stress, chaperone
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 29086.92

Authors

Vijayalakshmi, J.,Mukhergee, M.K.,Graumann, J.,Jakob, U.,Saper, M.A. (deposition date: 2001-01-09, release date: 2001-05-16, Last modification date: 2024-04-03)

Primary citation

Vijayalakshmi, J.,Mukhergee, M.K.,Graumann, J.,Jakob, U.,Saper, M.A.
The 2.2 A crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity.
Structure, 9:367-375, 2001

PubMed Abstract: One strategy that cells employ to respond to environmental stresses (temperature, oxidation, and pathogens) is to increase the expression of heat shock proteins necessary to maintain viability. Several heat shock proteins function as molecular chaperones by binding unfolded polypeptides and preventing their irreversible aggregation. Hsp33, a highly conserved bacterial heat shock protein, is a redox-regulated molecular chaperone that appears to protect cells against the lethal effects of oxidative stress.

PubMed: 11377197
DOI: 10.1016/S0969-2126(01)00597-4

Experimental method

X-RAY DIFFRACTION (2.2 Å)