Abstract
The X-ray crystal structure of the Escherichia coli stress response protein HDEA has been determined at 2.0 Å resolution. The single domain α-helical protein is found in the periplasmic space, where it supports an acid resistance phenotype essential for infectivity of enteric bacterial pathogens, such as Shigella and E. coli. Functional studies demonstrate that HDEA is activated by a dimer-to-monomer transition at acidic pH, leading to suppression of aggregation by acid-denatured proteins. We suggest that HDEA may support chaperone-like functions during the extremely acidic conditions. (C) 2000 Academic Press.
Original language | English (US) |
---|---|
Pages (from-to) | 605-612 |
Number of pages | 8 |
Journal | Journal of molecular biology |
Volume | 295 |
Issue number | 3 |
DOIs | |
State | Published - Jan 21 2000 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
Keywords
- Acid resistance
- Function
- HDEA
- Stress response
- Structure