3u2a: Difference between revisions
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< | ==Adaptor dependent degradation of a cell-cycle regulator reveals diversity in substrate architectures== | ||
<StructureSection load='3u2a' size='340' side='right'caption='[[3u2a]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3u2a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U2A 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]] 1.7Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</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=3u2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2a OCA], [https://pdbe.org/3u2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u2a RCSB], [https://www.ebi.ac.uk/pdbsum/3u2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u2a ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H3CDG5_CAUVN A0A0H3CDG5_CAUVN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In Caulobacter crescentus, the ClpXP protease degrades several crucial cell-cycle regulators, including the phosphodiesterase PdeA. Degradation of PdeA requires the response regulator CpdR and signals a morphological transition in concert with initiation of DNA replication. Here, we report the structure of a Per-Arnt-Sim (PAS) domain of PdeA and show that it is necessary for CpdR-dependent degradation in vivo and in vitro. CpdR acts as an adaptor, tethering the amino-terminal PAS domain to ClpXP and promoting recognition of the weak carboxyl-terminal degron of PdeA, a combination that ensures processive proteolysis. We identify sites on the PAS domain needed for CpdR recognition and find that one subunit of the PdeA dimer can be delivered to ClpXP by its partner. Finally, we show that improper stabilization of PdeA in vivo alters cellular behavior. These results introduce an adaptor/substrate pair for ClpXP and reveal broad diversity in adaptor-mediated proteolysis. | |||
Adaptor-dependent degradation of a cell-cycle regulator uses a unique substrate architecture.,Rood KL, Clark NE, Stoddard PR, Garman SC, Chien P Structure. 2012 Jul 3;20(7):1223-32. Epub 2012 Jun 7. PMID:22682744<ref>PMID:22682744</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
<div class="pdbe-citations 3u2a" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caulobacter vibrioides]] | [[Category: Caulobacter vibrioides]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Chien | [[Category: Chien P]] | ||
[[Category: Clark | [[Category: Clark NE]] | ||
[[Category: Garman | [[Category: Garman SC]] | ||
[[Category: Rood | [[Category: Rood K]] | ||
Latest revision as of 13:30, 6 November 2024
Adaptor dependent degradation of a cell-cycle regulator reveals diversity in substrate architecturesAdaptor dependent degradation of a cell-cycle regulator reveals diversity in substrate architectures
Structural highlights
FunctionPublication Abstract from PubMedIn Caulobacter crescentus, the ClpXP protease degrades several crucial cell-cycle regulators, including the phosphodiesterase PdeA. Degradation of PdeA requires the response regulator CpdR and signals a morphological transition in concert with initiation of DNA replication. Here, we report the structure of a Per-Arnt-Sim (PAS) domain of PdeA and show that it is necessary for CpdR-dependent degradation in vivo and in vitro. CpdR acts as an adaptor, tethering the amino-terminal PAS domain to ClpXP and promoting recognition of the weak carboxyl-terminal degron of PdeA, a combination that ensures processive proteolysis. We identify sites on the PAS domain needed for CpdR recognition and find that one subunit of the PdeA dimer can be delivered to ClpXP by its partner. Finally, we show that improper stabilization of PdeA in vivo alters cellular behavior. These results introduce an adaptor/substrate pair for ClpXP and reveal broad diversity in adaptor-mediated proteolysis. Adaptor-dependent degradation of a cell-cycle regulator uses a unique substrate architecture.,Rood KL, Clark NE, Stoddard PR, Garman SC, Chien P Structure. 2012 Jul 3;20(7):1223-32. Epub 2012 Jun 7. PMID:22682744[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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