ArticleActa crystallographica. Section D, Biological crystallography2015
A disulfide-bond cascade mechanism for arsenic(III) S-adenosylmethionine methyltransferase.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 50 citations in OpenAlex.
- Growth substrate limitation enhances anaerobic arsenic methylation byApplied and environmental microbiology · 2024Article
- Elucidating arsenic-bound proteins in the protein data bank: data mining and amino acid cross-validation through Raman spectroscopy.RSC advances · 2023Article
- Two-tiered mutualism improves survival and competitiveness of cross-feeding soil bacteria.The ISME journal · 2023Article
- Bifunctional protein ArsRBMC microbiology · 2023Article
- Functional characterization of the methylarsenite-inducible arsRM operon from Noviherbaspirillum denitrificans HC18.Environmental microbiology · 2022Article
- Identification of the Biosynthetic Gene Cluster for the Organoarsenical Antibiotic Arsinothricin.Microbiology spectrum · 2021Article
- Arsenic methylation - Lessons from three decades of research.Toxicology · 2021Review
- Arsenic toxicokinetic modeling and risk analysis: Progress, needs and applications.Toxicology · 2021Review
- Origins, fate, and actions of methylated trivalent metabolites of inorganic arsenic: progress and prospects.Archives of toxicology · 2021Review
- Semisynthesis of the Organoarsenical Antibiotic Arsinothricin.Journal of natural products · 2020Article
- Identification of Steps in the Pathway of Arsenosugar Biosynthesis.Environmental science & technology · 2019Article
- The Structure of an As(III) S-Adenosylmethionine Methyltransferase with 3-Coordinately Bound As(III) Depicts the First Step in Catalysis.Biochemistry · 2018Article
- Reorientation of the Methyl Group in MAs(III) is the Rate-Limiting Step in the ArsM As(III)ACS omega · 2018Article
- Arsenic methylation by a novel ArsM As(III) S-adenosylmethionine methyltransferase that requires only two conserved cysteine residues.Molecular microbiology · 2018Article
- Biochemical Characterization of ArsI: A Novel C-As Lyase for Degradation of Environmental Organoarsenicals.Environmental science & technology · 2017Article
- Recurrent horizontal transfer of arsenite methyltransferase genes facilitated adaptation of life to arsenic.Scientific reports · 2017Article
- Oncogenomic disruptions in arsenic-induced carcinogenesis.Oncotarget · 2017Review
- Conserved cysteine residues determine substrate specificity in a novel As(III) S-adenosylmethionine methyltransferase from Aspergillus fumigatus.Molecular microbiology · 2017Article
- Co-expression of Cyanobacterial Genes for Arsenic Methylation and Demethylation inFrontiers in microbiology · 2017Article
- The organoarsenical biocycle and the primordial antibiotic methylarsenite.Metallomics : integrated biometal science · 2016Review
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
Abstract
Methylation of the toxic metalloid arsenic is widespread in nature. Members of every kingdom have arsenic(III) S-adenosylmethionine (SAM) methyltransferase enzymes, which are termed ArsM in microbes and AS3MT in animals, including humans. Trivalent arsenic(III) is methylated up to three times to form methylarsenite [MAs(III)], dimethylarsenite [DMAs(III)] and the volatile trimethylarsine [TMAs(III)]. In microbes, arsenic methylation is a detoxification process. In humans, MAs(III) and DMAs(III) are more toxic and carcinogenic than either inorganic arsenate or arsenite. Here, new crystal structures are reported of ArsM from the thermophilic eukaryotic alga Cyanidioschyzon sp. 5508 (CmArsM) with the bound aromatic arsenicals phenylarsenite [PhAs(III)] at 1.80 Å resolution and reduced roxarsone [Rox(III)] at 2.25 Å resolution. These organoarsenicals are bound to two of four conserved cysteine residues: Cys174 and Cys224. The electron density extends the structure to include a newly identified conserved cysteine residue, Cys44, which is disulfide-bonded to the fourth conserved cysteine residue, Cys72. A second disulfide bond between Cys72 and Cys174 had been observed previously in a structure with bound SAM. The loop containing Cys44 and Cys72 shifts by nearly 6.5 Å in the arsenic(III)-bound structures compared with the SAM-bound structure, which suggests that this movement leads to formation of the Cys72-Cys174 disulfide bond. A model is proposed for the catalytic mechanism of arsenic(III) SAM methyltransferases in which a disulfide-bond cascade maintains the products in the trivalent state.
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