ArticleJournal of molecular modeling2019
Structure and function prediction of arsenate reductase from Deinococcus indicus DR1.
Article in Journal of molecular modeling, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Predicting the metalloproteome of Deinococcus indicus DR1 through integrative structure and function annotation.Biodegradation · 2026Article
- The Hypersaline Soils of the Odiel Saltmarshes Natural Area as a Source for Uncovering a New Taxon:Microorganisms · 2024Article
- A step into the rare biosphere: genomic features of the new genusFrontiers in microbiology · 2023Article
- Structural and functional mapping ofComputational and structural biotechnology journal · 2023Article
- Unraveling the multifaceted resilience of arsenic resistant bacteriumFrontiers in microbiology · 2023Article
- Phylogenetic analysis and characterization of arsenic (As) transforming bacterial marker proteins following isolation of As-tolerant indigenous bacteria.Archives of microbiology · 2022Article
- Biotin pathway in novelFrontiers in microbiology · 2022Article
- Biochemical, molecular and in silico characterization of arsenate reductase from Bacillus thuringiensis KPWP1 tolerant to salt, arsenic and a wide range of pH.Archives of microbiology · 2021Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arsenic prevalence in the environment impelled many organisms to develop resistance over the course of evolution. Tolerance to arsenic, either as the pentavalent [As(V)] form or the trivalent form [As(III)], by bacteria has been well studied in prokaryotes, and the mechanism of action is well defined. However, in the rod-shaped arsenic tolerant Deinococcus indicus DR1, the key enzyme, arsenate reductase (ArsC) has not been well studied. ArsC of D. indicus belongs to the Grx-linked prokaryotic arsenate reductase family. While it shares homology with the well-studied ArsC of Escherichia coli having a catalytic cysteine (Cys 12) and arginine triad (Arg 60, 94, and 107), the active site of D.indicus ArsC contains four residues Glu 9, Asp 53, Arg 86, and Glu 100, and with complete absence of structurally equivalent residue for crucial Cys 12. Here, we report that the mechanism of action of ArsC of D. indicus is different as a result of convergent evolution and most likely able to detoxify As(V) using a mix of positively- and negatively-charged residues in its active site, unlike the residues of E. coli. This suggests toward the possibility of an alternative mechanism of As (V) degradation in bacteria.
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