ArticleNature chemical biology2025
Complex structure and activation mechanism of arginine kinase McsB by McsA.
Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Structural Insights into Arginine Kinase and Phosphagen Kinase Homologs: Mechanisms of Catalysis, Regulation, and Evolution.Biology · 2025Review
- Conformational Dynamics and Structural Transitions of Arginine Kinase: Implications for Catalysis and Allergen Control.Life (Basel, Switzerland) · 2025Review
- De novo designed protein guiding targeted protein degradation.Nature communications · 2025Article
- Screening the Pandemic Response Box identifies novel ligands of the Staphylococcus aureus protein arginine kinase, McsB.Molecular biology reports · 2025Article
- Requirement of ClpX for CtsR dissociation from its operator elements upon heat stress inFrontiers in microbiology · 2025Article
Corrections and comments
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Authors and funding
19 authors.
Funding
Abstract
Protein phosphorylation is a pivotal post-translational modification modulating various cellular processes. In Gram-positive bacteria, the protein arginine kinase McsB, along with its activator McsA, has a key role in labeling misfolded and damaged proteins during stress. However, the activation mechanism of McsB by McsA remains elusive. Here we report the cryo-electron microscopy structure of a tetrameric McsA-McsB complex at 3.41 Å resolution. Biochemical analysis indicates that the homotetrameric assembly is essential for McsB's kinase activity. The conserved C-terminal zinc finger of McsA interacts with an extended loop in McsB, optimally orienting a critical catalytic cysteine residue. In addition, McsA binding decreases the CtsR's affinity for McsB, enhancing McsB's kinase activity and accelerating the turnover rate of CtsR phosphorylation. Furthermore, McsA binding also increases McsB's thermostability, ensuring its activity under heat stress. These findings elucidate the structural basis and activation mechanism of McsB in stress response.
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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.