Download MendeleyStructural features of halophilicity derived from the crystal structure of dihydrofolate reductase from the Dead Sea halophilic archaeon, Haloferax volcanii.
Pieper, U., Kapadia, G., Mevarech, M., Herzberg, O.(1998) Structure 6: 75-88
- PubMed: 9493269
- DOI: https://doi.org/10.1016/s0969-2126(98)00009-4
- Primary Citation of Related Structures:
1VDR - PubMed Abstract:
The proteins of halophilic archaea require high salt concentrations both for stability and for activity, whereas they denature at low ionic strength. The structural basis for this phenomenon is not yet well understood. The crystal structure of dihydrofolate reductase (DHFR) from Haloferax volcanii (hv-DHFR) reported here provides the third example of a structure of a protein from a halophilic organism. The enzyme is considered moderately halophilic, as it retains activity and secondary structure at monovalent salt concentrations as low as 0.5 M.
Organizational Affiliation:
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, MD 20850, USA.
