1VDR

DIHYDROFOLATE REDUCTASE

Summary for 1VDR

• Entry DOI: 10.2210/pdb1vdr/pdb
• Descriptor: DIHYDROFOLATE REDUCTASE, PHOSPHATE ION (3 entities in total)
• Functional Keywords: oxidoreductase, dihydrofolate reductase, halophilic enzyme
• Biological source: Haloferax volcanii
• Total number of polymer chains: 2
• Total formula weight: 36280.56

Authors

Pieper, U.,Herzberg, O. (deposition date: 1997-11-30, release date: 1998-02-25, Last modification date: 2024-05-22)

Primary citation

Pieper, U.,Kapadia, G.,Mevarech, M.,Herzberg, O.
Structural features of halophilicity derived from the crystal structure of dihydrofolate reductase from the Dead Sea halophilic archaeon, Haloferax volcanii.
Structure, 6:75-88, 1998

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.

PubMed: 9493269
DOI: 10.1016/S0969-2126(98)00009-4

Experimental method

X-RAY DIFFRACTION (2.55 Å)