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3j3s

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==Structural dynamics of the MecA-ClpC complex revealed by cryo-EM==
==Structural dynamics of the MecA-ClpC complex revealed by cryo-EM==
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<StructureSection load='3j3s' size='340' side='right' caption='[[3j3s]], [[Resolution|resolution]] 11.00&Aring;' scene=''>
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<SX load='3j3s' size='340' side='right' viewer='molstar' caption='[[3j3s]], [[Resolution|resolution]] 11.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3j3s]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J3S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J3S FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3j3s]] is a 12 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=3J3S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J3S FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j3r|3j3r]], [[3j3t|3j3t]], [[3j3u|3j3u]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 11&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mecA, BSU11520 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU]), clpC, mecB, BSU00860 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j3s OCA], [https://pdbe.org/3j3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j3s RCSB], [https://www.ebi.ac.uk/pdbsum/3j3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j3s ProSAT]</span></td></tr>
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<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=3j3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j3s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j3s RCSB], [http://www.ebi.ac.uk/pdbsum/3j3s PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/MECA1_BACSU MECA1_BACSU] Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation. Also involved in Spx degradation by ClpC.<ref>PMID:12598648</ref>
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The MecA-ClpC complex is a bacterial type II AAA+ molecular machine, responsible for regulated unfolding of substrates, such as transcription factors ComK and ComS, and targeting them to ClpP for degradation. The six subunits of the MecA-ClpC complex form a closed barrel-like structure, featured with three stacked rings and a hollow passage, where substrates are threaded and translocated through successive pores. Although the general concepts of how polypeptides are unfolded and translocated by internal pore loops of AAA+ proteins are long conceived, the detailed mechanistic model remains elusive. With cryo-electron microscopy, we captured four different structures of the MecA-ClpC complexes. These complexes differ in the nucleotide binding states of the two AAA+ rings, and therefore might presumably reflect distinctive, representative snapshots from a dynamic unfolding cycle of this hexameric complex. Structural analysis reveals that nucleotide binding and hydrolysis modulate the hexameric complex in a number of fashions, including the opening of the N-terminal ring, the axial and radial positions of pore loops, the compactness of the C-terminal ring, as well as the relative rotation between the two NBD rings. More importantly, our structural and biochemical data indicate there is an active allosteric communication between the two AAA+ rings, and suggest that concerted actions of two AAA+ rings are required for the efficiency of the substrate unfolding and translocation. These findings provide important mechanistic insights into the dynamic cycle of the MecA-ClpC unfoldase, and especially, lay a foundation toward the complete understanding of the structural dynamics of the general type II AAA+ hexamers.
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Structural dynamics of the MecA-ClpC complex: a type II AAA+ protein unfolding machine.,Liu J, Mei Z, Li N, Qi Y, Xu Y, Shi Y, Wang F, Lei J, Gao N J Biol Chem. 2013 Apr 17. PMID:23595989<ref>PMID:23595989</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Bacsu]]
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[[Category: Bacillus subtilis subsp. subtilis str. 168]]
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[[Category: Gao, N.]]
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[[Category: Large Structures]]
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[[Category: Lei, J.]]
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[[Category: Gao N]]
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[[Category: Li, N.]]
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[[Category: Lei J]]
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[[Category: Liu, J.]]
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[[Category: Li N]]
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[[Category: Mei, Z.]]
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[[Category: Liu J]]
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[[Category: Qi, Y.]]
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[[Category: Mei Z]]
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[[Category: Shi, Y.]]
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[[Category: Qi Y]]
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[[Category: Wang, F.]]
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[[Category: Shi Y]]
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[[Category: Xu, Y.]]
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[[Category: Wang F]]
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[[Category: Aaa+ atpase]]
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[[Category: Xu Y]]
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[[Category: Chaperone]]
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[[Category: Clpc]]
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[[Category: Meca]]
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[[Category: Protein unfolding]]
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Current revision

Structural dynamics of the MecA-ClpC complex revealed by cryo-EM

3j3s, resolution 11.00Å

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