5YVR
Crystal Structure of the H277A mutant of ADH/D1, an archaeal halo-thermophilic Red Sea brine pool alcohol dehydrogenase
Summary for 5YVR
| Entry DOI | 10.2210/pdb5yvr/pdb |
| Related | 5yvm |
| Descriptor | alcohol dehydrogenase, MANGANESE (II) ION, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | protein-cofactor complex, dehydrogenase, mutant, halophilic, thermophilic, oxidoreductase |
| Biological source | candidate divison MSBL1 archaeon SCGC-AAA259E19 |
| Total number of polymer chains | 1 |
| Total formula weight | 45102.17 |
| Authors | Groetzinger, S.W.,Strillinger, E.,Frank, A.,Eppinger, J.,Groll, M.,Arold, S.T. (deposition date: 2017-11-27, release date: 2017-12-27, Last modification date: 2023-11-22) |
| Primary citation | Groetzinger, S.W.,Karan, R.,Strillinger, E.,Bader, S.,Frank, A.,Al Rowaihi, I.S.,Akal, A.,Wackerow, W.,Archer, J.A.,Rueping, M.,Weuster-Botz, D.,Groll, M.,Eppinger, J.,Arold, S.T. Identification and Experimental Characterization of an Extremophilic Brine Pool Alcohol Dehydrogenase from Single Amplified Genomes ACS Chem. Biol., 13:161-170, 2018 Cited by PubMed Abstract: Because only 0.01% of prokaryotic genospecies can be cultured and in situ observations are often impracticable, culture-independent methods are required to understand microbial life and harness potential applications of microbes. Here, we report a methodology for the production of proteins with desired functions based on single amplified genomes (SAGs) from unculturable species. We use this method to resurrect an alcohol dehydrogenase (ADH/D1) from an uncharacterized halo-thermophilic archaeon collected from a brine pool at the bottom of the Red Sea. Our crystal structure of 5,6-dihydroxy NADPH-bound ADH/D1 combined with biochemical analyses reveal the molecular features of its halo-thermophily, its unique habitat adaptations, and its possible reaction mechanism for atypical oxygen activation. Our strategy offers a general guide for using SAGs as a source for scientific and industrial investigations of "microbial dark matter." PubMed: 29188989DOI: 10.1021/acschembio.7b00792 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.896 Å) |
Structure validation
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