Some Like It Hot –Structural Changes in Extremophile Rubredoxin at 120 °C
How does the structure of a protein change as the temperature is raised from cryogenic conditions at 100 K to 393 K? Understanding the structure and dynamics of proteins under environmental extremes is relevant for human health, biotechnological applications, and our search for life elsewhere in the universe. Here we reveal the high temperature crystal structure of a hyperthermophilic (Pyrococcus furiosus) rubredoxin at 393 K (120 °C), together with multiple complementary structures down to 100 K. The results are compared with molecular dynamics calculations. Significant changes in H-bonding are observed. Discussions about high-temperature protein structure and stability need to recognize that low temperature structures may not represent the high temperature case.
Authors
- Francis E. Jenney (ORCID: https://orcid.org/0000-0002-1667-6924)
- Stephen P. Cramer (ORCID: https://orcid.org/0000-0002-3751-7623)
- Igor Leontyev (ORCID: https://orcid.org/0009-0005-7468-4569)
- Darren S. A. George (ORCID: https://orcid.org/0009-0002-6548-2779)
- Tzanko Doukov (ORCID: https://orcid.org/0000-0001-8625-2572)
Institutions
- Philadelphia College of Osteopathic Medicine (US)
- SLAC National Accelerator Laboratory (US)
- Search for Extraterrestrial Intelligence (US)
Publication Details
- Journal
- Angewandte Chemie International Edition
- Published
- 2025-11-24
- DOI
- https://doi.org/10.1002/anie.202520302
- Citations
- 1
- Primary Topic
- Protein Structure and Dynamics
- Type
- article
- Field-Weighted Citation Impact
- 0.81
Funders
- National Science Foundation
- U.S. Department of Energy
- National Institutes of Health
- Office of Science
- National Institute of General Medical Sciences
- Basic Energy Sciences
- Biological and Environmental Research
- SLAC National Accelerator Laboratory