6fh4: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fh4 OCA], [http://pdbe.org/6fh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fh4 RCSB], [http://www.ebi.ac.uk/pdbsum/6fh4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fh4 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fh4 OCA], [http://pdbe.org/6fh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fh4 RCSB], [http://www.ebi.ac.uk/pdbsum/6fh4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fh4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Publication Abstract from PubMed == | |||
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. | |||
Structure of McsB, a protein kinase for regulated arginine phosphorylation.,Suskiewicz MJ, Hajdusits B, Beveridge R, Heuck A, Vu LD, Kurzbauer R, Hauer K, Thoeny V, Rumpel K, Mechtler K, Meinhart A, Clausen T Nat Chem Biol. 2019 Apr 8. pii: 10.1038/s41589-019-0265-y. doi:, 10.1038/s41589-019-0265-y. PMID:30962626<ref>PMID:30962626</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 6fh4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 09:48, 17 April 2019
CtsR C-terminal domain with bound phospho-arginineCtsR C-terminal domain with bound phospho-arginine
Structural highlights
Publication Abstract from PubMedProtein 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. Structure of McsB, a protein kinase for regulated arginine phosphorylation.,Suskiewicz MJ, Hajdusits B, Beveridge R, Heuck A, Vu LD, Kurzbauer R, Hauer K, Thoeny V, Rumpel K, Mechtler K, Meinhart A, Clausen T Nat Chem Biol. 2019 Apr 8. pii: 10.1038/s41589-019-0265-y. doi:, 10.1038/s41589-019-0265-y. PMID:30962626[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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