2OUI
D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica
Summary for 2OUI
| Entry DOI | 10.2210/pdb2oui/pdb |
| Related | 1Y9A |
| Descriptor | NADP-dependent alcohol dehydrogenase, ZINC ION, NITRATE ION, ... (10 entities in total) |
| Functional Keywords | tetramer, metal-binding, nadp, oxidoreductase, p275d mutation, cacodylate ion, thermosatbility |
| Biological source | Entamoeba histolytica |
| Cellular location | Cytoplasm: P35630 |
| Total number of polymer chains | 4 |
| Total formula weight | 157099.26 |
| Authors | Frolow, F.,Shimon, L.,Burstein, Y.,Goihberg, E.,Peretz, M.,Dym, O. (deposition date: 2007-02-11, release date: 2008-02-12, Last modification date: 2023-10-25) |
| Primary citation | 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 Cited by 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) DOI: 10.1002/prot.21946 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.77 Å) |
Structure validation
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