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| | <StructureSection load='3pxg' size='340' side='right'caption='[[3pxg]], [[Resolution|resolution]] 3.65Å' scene=''> | | <StructureSection load='3pxg' size='340' side='right'caption='[[3pxg]], [[Resolution|resolution]] 3.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pxg]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3pxg]] is a 12 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=3PXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXG FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2y1q|2y1q]], [[2y1r|2y1r]], [[3pxi|3pxi]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.654Å</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=3pxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pxg OCA], [https://pdbe.org/3pxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pxg RCSB], [https://www.ebi.ac.uk/pdbsum/3pxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pxg ProSAT]</span></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=3pxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pxg OCA], [https://pdbe.org/3pxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pxg RCSB], [https://www.ebi.ac.uk/pdbsum/3pxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pxg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> [[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.
| + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mei, Z Q]] | + | [[Category: Mei ZQ]] |
| - | [[Category: Shi, Y G]] | + | [[Category: Shi YG]] |
| - | [[Category: Wang, F]] | + | [[Category: Wang F]] |
| - | [[Category: Wang, J W]] | + | [[Category: Wang JW]] |
| - | [[Category: Aaa+ protein]]
| + | |
| - | [[Category: Clpb]]
| + | |
| - | [[Category: Clpc]]
| + | |
| - | [[Category: Clpx]]
| + | |
| - | [[Category: Hsp100/clp]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Proteolysis]]
| + | |
| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schlothauer T, Mogk A, Dougan DA, Bukau B, Turgay K. MecA, an adaptor protein necessary for ClpC chaperone activity. Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2306-11. Epub 2003 Feb 21. PMID:12598648 doi:10.1073/pnas.0535717100
- ↑ Wang F, Mei Z, Qi Y, Yan C, Hu Q, Wang J, Shi Y. Structure and mechanism of the hexameric MecA-ClpC molecular machine. Nature. 2011 Mar 2. PMID:21368759 doi:10.1038/nature09780
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