2NVB
Contribution of Pro275 to the Thermostability of the Alcohol Dehydrogenases (ADHs)
Summary for 2NVB
| Entry DOI | 10.2210/pdb2nvb/pdb |
| Related | 1YKF |
| Descriptor | NADP-dependent alcohol dehydrogenase, ZINC ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | rossmann fold, structural genomics, israel structural proteomics center, ispc, oxidoreductase |
| Biological source | Thermoanaerobacter brockii |
| Total number of polymer chains | 4 |
| Total formula weight | 154086.63 |
| Authors | Goihberg, E.,Tel-Or, S.,Peretz, M.,Frolow, F.,Dym, O.,Burstein, Y.,Israel Structural Proteomics Center (ISPC) (deposition date: 2006-11-12, release date: 2007-11-13, 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 (2.8 Å) |
Structure validation
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