View source for 5hbn


==ClpC N-terminal domain with bound phospho-arginine==
<StructureSection load='5hbn' size='340' side='right'caption='[[5hbn]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hbn]] is a 1 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=5HBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HBN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.602&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=RPI:PHOSPHO-ARGININE'>RPI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5hbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hbn OCA], [https://pdbe.org/5hbn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hbn RCSB], [https://www.ebi.ac.uk/pdbsum/5hbn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hbn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CLPC_BACSU CLPC_BACSU] Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein turnover is a tightly controlled process critical for the removal of aberrant polypeptides and for cellular signalling. Whereas ubiquitin marks eukaryotic proteins for proteasomal degradation, a general tagging system for the equivalent bacterial Clp proteases is not known. Here we address the targeting mechanism of the ClpC:ClpP proteolytic complex from Bacillus subtilis. Quantitative affinity proteomics using a ClpP trapping mutant show that proteins phosphorylated on arginine residues are selectively targeted to ClpC:ClpP. In vitro reconstitution experiments reveal that the McsB-mediated arginine phosphorylation is required and sufficient for the degradation of substrate proteins. The docking site for phosphoarginine is located in the N-terminal domain of the ClpC ATPase as resolved at high resolution in a co-crystal structure. Together, our data demonstrate that pArg functions as a bona fide degradation tag for the ClpC:ClpP protease. This system, widely distributed across Gram-positive bacteria, is functionally analogous to the eukaryotic ubiquitin-proteasome system.

Arginine phosphorylation marks proteins for degradation by a Clp protease.,Trentini DB, Suskiewicz MJ, Heuck A, Kurzbauer R, Deszcz L, Mechtler K, Clausen T Nature. 2016 Oct 6. doi: 10.1038/nature20122. PMID:27749819<ref>PMID:27749819</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hbn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Clausen T]]
[[Category: Suskiewicz MJ]]