Structural highlights
Function
A0A133UP32_9EURY
Publication Abstract from PubMed
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."
Identification and Experimental Characterization of an Extremophilic Brine Pool Alcohol Dehydrogenase from Single Amplified Genomes.,Grotzinger SW, Karan R, Strillinger E, Bader S, Frank A, Al Rowaihi IS, Akal A, Wackerow W, Archer JA, Rueping M, Weuster-Botz D, Groll M, Eppinger J, Arold ST ACS Chem Biol. 2017 Dec 18. doi: 10.1021/acschembio.7b00792. PMID:29188989[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Grotzinger SW, Karan R, Strillinger E, Bader S, Frank A, Al Rowaihi IS, Akal A, Wackerow W, Archer JA, Rueping M, Weuster-Botz D, Groll M, Eppinger J, Arold ST. Identification and Experimental Characterization of an Extremophilic Brine Pool Alcohol Dehydrogenase from Single Amplified Genomes. ACS Chem Biol. 2017 Dec 18. doi: 10.1021/acschembio.7b00792. PMID:29188989 doi:http://dx.doi.org/10.1021/acschembio.7b00792