ArticleBiochemistry2018
The Structure of an As(III) S-Adenosylmethionine Methyltransferase with 3-Coordinately Bound As(III) Depicts the First Step in Catalysis.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 40 citations in OpenAlex.
- Synergistic function of ars genes in arsenic detoxification and biosynthesis of organoarsenicals.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Review
- AsJournal of the American Chemical Society · 2024Article
- Soil redox status governs within-field spatial variation in microbial arsenic methylation and rice straighthead disease.The ISME journal · 2024Article
- Effects of Dietary Intake of Arsenosugars and Other Organic Arsenic Species on Studies of Arsenic Methylation Efficiency in Humans.Environment & health (Washington, D.C.) · 2023Review
- Arsenite Methyltransferase Diversity and Optimization of Methylation Efficiency.Environmental science & technology · 2023Article
- Tristhiolato Pseudopeptides Bind Arsenic(III) in an AsSInorganic chemistry · 2023Article
- Transcriptional Control ofApplied and environmental microbiology · 2023Article
- Arsenic 3 methyltransferase (AS3MT) automethylates on cysteine residues in vitro.Archives of toxicology · 2022Article
- Functional characterization of the methylarsenite-inducible arsRM operon from Noviherbaspirillum denitrificans HC18.Environmental microbiology · 2022Article
- 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
- Density Functional Theory Investigation of As(III) S-Adenosylmethionine Methyltransferase.ACS omega · 2020Article
- Recent Advances in Arsenic Research: Significance of Differential Susceptibility and Sustainable Strategies for Mitigation.Frontiers in public health · 2020Review
- The Human Gut Microbiome's Influence on Arsenic Toxicity.Current pharmacology reports · 2019Article
- Insights into S-adenosyl-l-methionine (SAM)-dependent methyltransferase related diseases and genetic polymorphisms.Mutation research. Reviews in mutation researchReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Arsenic is a ubiquitous environmental toxic substance and a Class 1 human carcinogen. Arsenic methylation by the enzyme As(III) S-adenosylmethionine (SAM) methyltransferase (ArsM in microbes or AS3MT in animals) detoxifies As(III) in microbes but transforms it into more toxic and potentially more carcinogenic methylated species in humans. We previously proposed a reaction pathway for ArsM/AS3MT that involves initial 3-coordinate binding of As(III). To date, reported structures have had only 2-coordinately bound trivalent arsenicals. Here we report a crystal structure of CmArsM from Cyanidioschyzon sp.5508 in which As(III) is 3-coordinately bound to three conserved cysteine residues with a molecule of the product S-adenosyl-l-homocysteine bound in the SAM binding site. We propose that this structure represents the first step in the catalytic cycle. In a previously reported SAM-bound structure, a disulfide bond is formed between two conserved cysteine residues. Comparison of these two structures indicates that there is a conformational change in the N-terminal domain of CmArsM that moves a loop to allow formation of the 3-coordinate As(III) binding site. We propose that this conformational change is an initial step in the As(III) SAM methyltransferase catalytic cycle.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.