3pxi: Difference between revisions

Latest revision as of 17:08, 1 November 2023

Structure of MecA108:ClpC

Structural highlights

3pxi is a 6 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 6.926Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[1]

[2]

@@ Line 3: / Line 3: @@
 <StructureSection load='3pxi' size='340' side='right'caption='[[3pxi]], [[Resolution|resolution]] 6.93&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3pxi]] is a 6 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=3PXI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3pxi]] is a 6 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=3PXI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXI 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]], [[3pxg|3pxg]]</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]] 6.926&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mecA, BSU11520 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835]), clpC, mecB, BSU00860 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=3pxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pxi OCA], [https://pdbe.org/3pxi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pxi RCSB], [https://www.ebi.ac.uk/pdbsum/3pxi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pxi ProSAT]</span></td></tr>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Vibrio subtilis ehrenberg 1835]]
+[[Category: Bacillus subtilis]]
 [[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]]

3pxi: Difference between revisions

Latest revision as of 17:08, 1 November 2023

Structure of MecA108:ClpC

Structural highlights

Function

Publication Abstract from PubMed

References

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