ArticleNature chemical biology2019
Structure of McsB, a protein kinase for regulated arginine phosphorylation.
Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Pushing the limits of single-cell proteomics to investigate bacterial heterogeneity using bacSCP.Nature communications · 2026Article
- Let the peptides shine: SOX (Sulfonamido-OXine)-labelled peptides for direct kinase and phosphatase monitoring.RSC chemical biology · 2026Review
- Decoding protein N-phosphorylation functionality and sequence patterns.Briefings in bioinformatics · 2025Article
- Structural and evolutionary insights into understudied bacterial serine-threonine pseudokinase families.Biochemical Society transactions · 2025Review
- Conformational Dynamics and Structural Transitions of Arginine Kinase: Implications for Catalysis and Allergen Control.Life (Basel, Switzerland) · 2025Review
- Complex structure and activation mechanism of arginine kinase McsB by McsA.Nature chemical biology · 2025Article
- Article
- A comprehensive review of arginine kinase proteins: What we need to know?Biochemistry and biophysics reports · 2024Review
- Arginine Kinase Activates Arginine for Phosphorylation by Pyramidalization and Polarization.ACS catalysis · 2024Article
- Structural insights into the regulation of protein-arginine kinase McsB by McsA.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Phosphoproteomic analysis reveals changes in A-Raf-related protein phosphorylation in response to Toxoplasma gondii infection in porcine macrophages.Parasites & vectors · 2024Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- A Review of the Bacterial Phosphoproteomes of Beneficial Microbes.Microorganisms · 2023Review
- A Perspective on Newly Emerging Proteolysis-Targeting Strategies in Antimicrobial Drug Discovery.Antibiotics (Basel, Switzerland) · 2022Review
- Identification of Arginine Phosphorylation in Mycolicibacterium smegmatis.Microbiology spectrum · 2022Article
- Article
- Applications of Bacterial Degrons and Degraders - Toward Targeted Protein Degradation in Bacteria.Frontiers in molecular biosciences · 2021Review
- Multiscale computation delivers organophosphorus reactivity and stereoselectivity to immunoglobulin scavengers.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Combining free energy calculations with tailored enzyme activity assays to elucidate substrate binding of a phospho-lysine phosphatase.Chemical science · 2020Article
- The Involvement of the McsB Arginine Kinase in Clp-Dependent Degradation of the MgsR Regulator inFrontiers in microbiology · 2020Article
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12 authors at 3 institutions in 2 countries.
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Abstract
Protein phosphorylation regulates key processes in all organisms. In Gram-positive bacteria, protein arginine phosphorylation plays a central role in protein quality control by regulating transcription factors and marking aberrant proteins for degradation. Here, we report structural, biochemical, and in vivo data of the responsible kinase, McsB, the founding member of an arginine-specific class of protein kinases. McsB differs in structure and mechanism from protein kinases that act on serine, threonine, and tyrosine residues and instead has a catalytic domain related to that of phosphagen kinases (PhKs), metabolic enzymes that phosphorylate small guanidino compounds. In McsB, the PhK-like phosphotransferase domain is structurally adapted to target protein substrates and is accompanied by a novel phosphoarginine (pArg)-binding domain that allosterically controls protein kinase activity. The identification of distinct pArg reader domains in this study points to a remarkably complex signaling system, thus challenging simplistic views of bacterial protein phosphorylation.
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