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Structure of McsB, a protein kinase for regulated arginine phosphorylation

(2019) Nature Chemical Biology. 15(5). p.510-518
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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.
Keywords
Cell Biology, Molecular Biology

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Chicago
Suskiewicz, Marcin J., Bence Hajdusits, Rebecca Beveridge, Alexander Heuck, Lam Dai Vu, Robert Kurzbauer, Katja Hauer, et al. 2019. “Structure of McsB, a Protein Kinase for Regulated Arginine Phosphorylation.” Nature Chemical Biology 15 (5): 510–518.
APA
Suskiewicz, M. J., Hajdusits, B., Beveridge, R., Heuck, A., Vu, L. D., Kurzbauer, R., Hauer, K., et al. (2019). Structure of McsB, a protein kinase for regulated arginine phosphorylation. Nature Chemical Biology, 15(5), 510–518.
Vancouver
1.
Suskiewicz MJ, Hajdusits B, Beveridge R, Heuck A, Vu LD, Kurzbauer R, et al. Structure of McsB, a protein kinase for regulated arginine phosphorylation. Nature Chemical Biology. Springer Nature; 2019;15(5):510–8.
MLA
Suskiewicz, Marcin J. et al. “Structure of McsB, a Protein Kinase for Regulated Arginine Phosphorylation.” Nature Chemical Biology 15.5 (2019): 510–518. Print.
@article{8613964,
  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.},
  author       = {Suskiewicz, Marcin J. and Hajdusits, Bence and Beveridge, Rebecca and Heuck, Alexander and Vu, Lam Dai and Kurzbauer, Robert and Hauer, Katja and Thoeny, Vanessa and Rumpel, Klaus and Mechtler, Karl and Meinhart, Anton and Clausen, Tim},
  issn         = {1552-4450},
  journal      = {Nature Chemical Biology},
  number       = {5},
  pages        = {510--518},
  publisher    = {Springer Nature},
  title        = {Structure of McsB, a protein kinase for regulated arginine phosphorylation},
  url          = {http://dx.doi.org/10.1038/s41589-019-0265-y},
  volume       = {15},
  year         = {2019},
}

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