ArticleProceedings of the National Academy of Sciences of the United States of America2007
Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 133 citations in OpenAlex.
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- The Potential of a Protein Model Synthesized Absent of Methionine.Molecules (Basel, Switzerland) · 2022Review
- Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity.International journal of molecular sciences · 2021Review
- Deletion of both methionine sulfoxide reductase A and methionine sulfoxide reductase C genes renders Salmonella Typhimurium highly susceptible to hypochlorite stress and poultry macrophages.Molecular biology reports · 2021Article
- Unique Cellular and Biochemical Features of Human Mitochondrial Peroxiredoxin 3 Establish the Molecular Basis for Its Specific Reaction with Thiostrepton.Antioxidants (Basel, Switzerland) · 2021Article
- Methionine Redox Homeostasis in Protein Quality Control.Frontiers in molecular biosciences · 2021Review
- Ionizing Radiation-induced Proteomic Oxidation inMolecular & cellular proteomics : MCP · 2020Article
- Reduction of Protein Bound Methionine Sulfoxide by a Periplasmic Dimethyl Sulfoxide Reductase.Antioxidants (Basel, Switzerland) · 2020Article
- X-ray absorption spectroscopy of organic sulfoxides.RSC advances · 2020Article
- Methionine Availability in the Arthropod Intestine Is Elucidated through Identification of Vibrio cholerae Methionine Acquisition Systems.Applied and environmental microbiology · 2020Article
- Methionine sulfoxide reductase B fromThe Journal of biological chemistry · 2020Article
- Upregulation of PBP1B and LpoB inAntimicrobial agents and chemotherapy · 2019Article
- Regulation of Gene Expression of Methionine Sulfoxide Reductases and Their New Putative Roles in Plants.International journal of molecular sciences · 2019Article
- The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function.Antioxidants (Basel, Switzerland) · 2018Review
6 more citing papers are in PubMed but not listed here.
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6 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The reduction of methionine sulfoxide (MetO) is mediated by methionine sulfoxide reductases (Msr). The MsrA and MsrB families can reduce free MetO and MetO within a peptide or protein context. This process is stereospecific with the S- and R-forms of MetO repaired by MsrA and MsrB, respectively. Cell extracts from an MsrA(-)B(-) knockout of Escherichia coli have several remaining Msr activities. This study has identified an enzyme specific for the free form of Met-(R)-O, fRMsr, through proteomic analysis. The recombinant enzyme exhibits the same substrate specificity and is as active as MsrA family members. E. coli fRMsr is, however, 100- to 1,000-fold more active than non-selenocysteine-containing MsrB enzymes for free Met-(R)-O. The crystal structure of E. coli fRMsr was previously determined, but no known function was assigned. Thus, the function of this protein has now been determined. The structural similarity of the E. coli and yeast proteins suggests that most fRMsrs use three cysteine residues for catalysis and the formation of a disulfide bond to enclose a small active site cavity. This latter feature is most likely a key determinant of substrate specificity. Moreover, E. coli fRMsr is the first GAF domain family member to show enzymatic activity. Other GAF domain proteins substitute the Cys residues and others to specifically bind cyclic nucleotides, chromophores, and many other ligands for signal potentiation. Therefore, Met-(R)-O may represent a signaling molecule in response to oxidative stress and nutrients via the TOR pathway in some organisms.
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