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==Adaptor dependent degradation of a cell-cycle regulator reveals diversity in substrate architectures== | ==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=''> | <StructureSection load='3u2a' size='340' side='right' caption='[[3u2a]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3u2a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3u2a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cauce Cauce]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U2A FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CC3396(PdeA), CC_3396 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CC3396(PdeA), CC_3396 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 CAUCE])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclic-guanylate-specific_phosphodiesterase Cyclic-guanylate-specific phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.52 3.1.4.52] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclic-guanylate-specific_phosphodiesterase Cyclic-guanylate-specific phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.52 3.1.4.52] </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=3u2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u2a RCSB], [http://www.ebi.ac.uk/pdbsum/3u2a PDBsum]</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=3u2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2a OCA], [http://pdbe.org/3u2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u2a RCSB], [http://www.ebi.ac.uk/pdbsum/3u2a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u2a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3u2a" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Cauce]] | ||
[[Category: Cyclic-guanylate-specific phosphodiesterase]] | [[Category: Cyclic-guanylate-specific phosphodiesterase]] | ||
[[Category: Chien, P]] | [[Category: Chien, P]] | ||
Revision as of 22:03, 11 August 2016
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
Publication 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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