2OUI

D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica

2OUI の概要

• エントリーDOI: 10.2210/pdb2oui/pdb
• 関連するPDBエントリー: 1Y9A
• 分子名称: NADP-dependent alcohol dehydrogenase, ZINC ION, NITRATE ION, ... (10 entities in total)
• 機能のキーワード: tetramer, metal-binding, nadp, oxidoreductase, p275d mutation, cacodylate ion, thermosatbility
• 由来する生物種: Entamoeba histolytica
• 細胞内の位置: Cytoplasm: P35630
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 157099.26

構造登録者

Frolow, F.,Shimon, L.,Burstein, Y.,Goihberg, E.,Peretz, M.,Dym, O. (登録日: 2007-02-11, 公開日: 2008-02-12, 最終更新日: 2023-10-25)

主引用文献

Goihberg, E.,Dym, O.,Tel-Or, S.,Shimon, L.,Frolow, F.,Peretz, M.,Burstein, Y.
Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution.
Proteins, 72:711-719, 2008

PubMed Abstract: Analysis of the three-dimensional structures of two closely related thermophilic and hyperthermophilic alcohol dehydrogenases (ADHs) from the respective microorganisms Entamoeba histolytica (EhADH1) and Thermoanaerobacter brockii (TbADH) suggested that a unique, strategically located proline residue (Pro275) at the center of the dimerization interface might be crucial for maintaining the thermal stability of TbADH. To assess the contribution of Pro275 to the thermal stability of the ADHs, we applied site-directed mutagenesis to replace Asp275 of EhADH1 with Pro (D275P-EhADH1) and conversely Pro275 of TbADH with Asp (P275D-TbADH). The results indicate that replacing Asp275 with Pro significantly enhances the thermal stability of EhADH1 (DeltaT(1/2) PubMed: 18260103
DOI: 10.1002/prot.21946

実験手法

X-RAY DIFFRACTION (1.77 Å)