6tv6

From Proteopedia

(Difference between revisions)

Current revision

Octameric McsB from Bacillus subtilis.

Structural highlights

6tv6 is a 4 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MCSB_BACSU Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix-turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under stress conditions. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity. Functions as an adapter whose kinase activity is required for ClpCP-mediated degradation of CtsR during heat stress. Is required for the delocalization of competence proteins from the cell poles, probably via a role in the degradation of anchor proteins.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

In Gram-positive bacteria, the McsB protein arginine kinase is central to protein quality control, labeling aberrant molecules for degradation by the ClpCP protease. Despite its importance for stress response and pathogenicity, it is still elusive how the bacterial degradation labeling is regulated. Here, we delineate the mechanism how McsB targets aberrant proteins during stress conditions. Structural data reveal a self-compartmentalized kinase, in which the active sites are sequestered in a molecular cage. The 'closed' octamer interconverts with other oligomers in a phosphorylation-dependent manner and, unlike these 'open' forms, preferentially labels unfolded proteins. In vivo data show that heat-shock triggers accumulation of higher order oligomers, of which the octameric McsB is essential for surviving stress situations. The interconversion of open and closed oligomers represents a distinct regulatory mechanism of a degradation labeler, allowing the McsB kinase to adapt its potentially dangerous enzyme function to the needs of the bacterial cell.

McsB forms a gated kinase chamber to mark aberrant bacterial proteins for degradation.,Hajdusits B, Suskiewicz MJ, Hundt N, Meinhart A, Kurzbauer R, Leodolter J, Kukura P, Clausen T Elife. 2021 Jul 30;10. pii: 63505. doi: 10.7554/eLife.63505. PMID:34328418^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hahn J, Kramer N, Briley K Jr, Dubnau D. McsA and B mediate the delocalization of competence proteins from the cell poles of Bacillus subtilis. Mol Microbiol. 2009 Apr;72(1):202-15. doi: 10.1111/j.1365-2958.2009.06636.x. Epub, 2009 Feb 17. PMID:19226326 doi:http://dx.doi.org/10.1111/j.1365-2958.2009.06636.x
↑ Elsholz AK, Hempel K, Michalik S, Gronau K, Becher D, Hecker M, Gerth U. Activity control of the ClpC adaptor McsB in Bacillus subtilis. J Bacteriol. 2011 Aug;193(15):3887-93. doi: 10.1128/JB.00079-11. Epub 2011 May, 27. PMID:21622759 doi:http://dx.doi.org/10.1128/JB.00079-11
↑ Elsholz AK, Turgay K, Michalik S, Hessling B, Gronau K, Oertel D, Mader U, Bernhardt J, Becher D, Hecker M, Gerth U. Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis. Proc Natl Acad Sci U S A. 2012 May 8;109(19):7451-6. doi:, 10.1073/pnas.1117483109. Epub 2012 Apr 19. PMID:22517742 doi:http://dx.doi.org/10.1073/pnas.1117483109
↑ Schmidt A, Trentini DB, Spiess S, Fuhrmann J, Ammerer G, Mechtler K, Clausen T. Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response. Mol Cell Proteomics. 2014 Feb;13(2):537-50. doi: 10.1074/mcp.M113.032292. Epub, 2013 Nov 20. PMID:24263382 doi:http://dx.doi.org/10.1074/mcp.M113.032292
↑ Suskiewicz MJ, Hajdusits B, Beveridge R, Heuck A, Vu LD, Kurzbauer R, Hauer K, Thoeny V, Rumpel K, Mechtler K, Meinhart A, Clausen T. Structure of McsB, a protein kinase for regulated arginine phosphorylation. Nat Chem Biol. 2019 Apr 8. pii: 10.1038/s41589-019-0265-y. doi:, 10.1038/s41589-019-0265-y. PMID:30962626 doi:http://dx.doi.org/10.1038/s41589-019-0265-y
↑ Hajdusits B, Suskiewicz MJ, Hundt N, Meinhart A, Kurzbauer R, Leodolter J, Kukura P, Clausen T. McsB forms a gated kinase chamber to mark aberrant bacterial proteins for degradation. Elife. 2021 Jul 30;10. pii: 63505. doi: 10.7554/eLife.63505. PMID:34328418 doi:http://dx.doi.org/10.7554/eLife.63505

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6tv6"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6tv6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TV6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RPI:PHOSPHO-ARGININE'>RPI</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RPI:PHOSPHO-ARGININE'>RPI</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6tv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tv6 OCA], [https://pdbe.org/6tv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tv6 RCSB], [https://www.ebi.ac.uk/pdbsum/6tv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tv6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/MCSB_BACSU MCSB_BACSU]] Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix-turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under stress conditions. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity. Functions as an adapter whose kinase activity is required for ClpCP-mediated degradation of CtsR during heat stress. Is required for the delocalization of competence proteins from the cell poles, probably via a role in the degradation of anchor proteins.<ref>PMID:19226326</ref> <ref>PMID:21622759</ref> <ref>PMID:22517742</ref> <ref>PMID:24263382</ref> <ref>PMID:30962626</ref>
+[https://www.uniprot.org/uniprot/MCSB_BACSU MCSB_BACSU] Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix-turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under stress conditions. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity. Functions as an adapter whose kinase activity is required for ClpCP-mediated degradation of CtsR during heat stress. Is required for the delocalization of competence proteins from the cell poles, probably via a role in the degradation of anchor proteins.<ref>PMID:19226326</ref> <ref>PMID:21622759</ref> <ref>PMID:22517742</ref> <ref>PMID:24263382</ref> <ref>PMID:30962626</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

6tv6

From Proteopedia

Current revision

Octameric McsB from Bacillus subtilis.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox