1VDR
DIHYDROFOLATE REDUCTASE
1VDR の概要
エントリーDOI | 10.2210/pdb1vdr/pdb |
分子名称 | DIHYDROFOLATE REDUCTASE, PHOSPHATE ION (3 entities in total) |
機能のキーワード | oxidoreductase, dihydrofolate reductase, halophilic enzyme |
由来する生物種 | Haloferax volcanii |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 36280.56 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 9493269DOI: 10.1016/S0969-2126(98)00009-4 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.55 Å) |
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