2y1q: Difference between revisions
New page: '''Unreleased structure''' The entry 2y1q is ON HOLD Authors: Wang, F., Mei, Z.Q., Wang, J.W., Shi, Y.G. Description: Crystal Structure of ClpC N-terminal Domain ''Page seeded by [htt... |
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==Crystal Structure of ClpC N-terminal Domain== | |||
<StructureSection load='2y1q' size='340' side='right'caption='[[2y1q]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2y1q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y1Q 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]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=2y1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y1q OCA], [https://pdbe.org/2y1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y1q RCSB], [https://www.ebi.ac.uk/pdbsum/2y1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y1q 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 == | |||
Regulated proteolysis by ATP-dependent proteases is universal in all living cells. Bacterial ClpC, a member of the Clp/Hsp100 family of AAA+ proteins (ATPases associated with diverse cellular activities) with two nucleotide-binding domains (D1 and D2), requires the adaptor protein MecA for activation and substrate targeting. The activated, hexameric MecA-ClpC molecular machine harnesses the energy of ATP binding and hydrolysis to unfold specific substrate proteins and translocate the unfolded polypeptide to the ClpP protease for degradation. Here we report three related crystal structures: a heterodimer between MecA and the amino domain of ClpC, a heterododecamer between MecA and D2-deleted ClpC, and a hexameric complex between MecA and full-length ClpC. In conjunction with biochemical analyses, these structures reveal the organizational principles behind the hexameric MecA-ClpC complex, explain the molecular mechanisms for MecA-mediated ClpC activation and provide mechanistic insights into the function of the MecA-ClpC molecular machine. These findings have implications for related Clp/Hsp100 molecular machines. | |||
Structure and mechanism of the hexameric MecA-ClpC molecular machine.,Wang F, Mei Z, Qi Y, Yan C, Hu Q, Wang J, Shi Y Nature. 2011 Mar 2. PMID:21368759<ref>PMID:21368759</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2y1q" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | |||
[[Category: Large Structures]] | |||
[[Category: Mei ZQ]] | |||
[[Category: Shi YG]] | |||
[[Category: Wang F]] | |||
[[Category: Wang JW]] | |||
Latest revision as of 17:01, 1 February 2024
Crystal Structure of ClpC N-terminal DomainCrystal Structure of ClpC N-terminal Domain
Structural highlights
FunctionCLPC_BACSU Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK. Publication Abstract from PubMedRegulated proteolysis by ATP-dependent proteases is universal in all living cells. Bacterial ClpC, a member of the Clp/Hsp100 family of AAA+ proteins (ATPases associated with diverse cellular activities) with two nucleotide-binding domains (D1 and D2), requires the adaptor protein MecA for activation and substrate targeting. The activated, hexameric MecA-ClpC molecular machine harnesses the energy of ATP binding and hydrolysis to unfold specific substrate proteins and translocate the unfolded polypeptide to the ClpP protease for degradation. Here we report three related crystal structures: a heterodimer between MecA and the amino domain of ClpC, a heterododecamer between MecA and D2-deleted ClpC, and a hexameric complex between MecA and full-length ClpC. In conjunction with biochemical analyses, these structures reveal the organizational principles behind the hexameric MecA-ClpC complex, explain the molecular mechanisms for MecA-mediated ClpC activation and provide mechanistic insights into the function of the MecA-ClpC molecular machine. These findings have implications for related Clp/Hsp100 molecular machines. Structure and mechanism of the hexameric MecA-ClpC molecular machine.,Wang F, Mei Z, Qi Y, Yan C, Hu Q, Wang J, Shi Y Nature. 2011 Mar 2. PMID:21368759[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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