8P5N
Arsenate reductase (ArsC2) from Deinococcus indicus, co-crystallized with arsenate
Summary for 8P5N
Entry DOI | 10.2210/pdb8p5n/pdb |
Descriptor | Low molecular weight phosphatase family protein, ARSENATE, GLYCEROL, ... (4 entities in total) |
Functional Keywords | bioremediation, arsenic, lmw-ptpase, reductase, oxidoreductase |
Biological source | Deinococcus indicus |
Total number of polymer chains | 2 |
Total formula weight | 31983.62 |
Authors | Gouveia, A.G.,Matias, P.M.,Romao, C.V. (deposition date: 2023-05-24, release date: 2023-08-30, Last modification date: 2024-11-20) |
Primary citation | Gouveia, A.G.,Salgueiro, B.A.,Ranmar, D.O.,Antunes, W.D.T.,Kirchweger, P.,Golani, O.,Wolf, S.G.,Elbaum, M.,Matias, P.M.,Romao, C.V. Unraveling the multifaceted resilience of arsenic resistant bacterium Deinococcus indicus . Front Microbiol, 14:1240798-1240798, 2023 Cited by PubMed Abstract: Arsenic (As) is a toxic heavy metal widely found in the environment that severely undermines the integrity of water resources. Bioremediation of toxic compounds is an appellative sustainable technology with a balanced cost-effective setup. To pave the way for the potential use of an arsenic resistant bacterium, as a platform for arsenic bioremediation, an extensive characterization of its resistance to cellular insults is paramount. A comparative analysis of cells grown in two rich nutrient media conditions (M53 and TGY) revealed distinct resistance patterns when cells are subjected to stress via UV-C and methyl viologen (MV). Cells grown in M53 demonstrated higher resistance to both UV-C and MV. Moreover, cells grow to higher density upon exposure to 25 mM As(V) in M53 in comparison with TGY. This analysis is pivotal for the culture of microbial species in batch culture bioreactors for bioremediation purposes. We also demonstrate for the first time the presence of polyphosphate granules in which are also found in a few species. To extend our analysis, we also characterized ArsC2 (arsenate reductase) involved in arsenic detoxification and structurally determined different states, revealing the structural evidence for a catalytic cysteine triple redox system. These results contribute for our understanding into the resistance mechanism against stress conditions. PubMed: 37692390DOI: 10.3389/fmicb.2023.1240798 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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