6emw

From Proteopedia

(Difference between revisions)

Revision as of 06:55, 24 October 2018

Structure of S.aureus ClpC in complex with MecA

Structural highlights

6emw is a 42 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885 and Staab. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	CA803_07045 ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885), clpC, BN1321_130009 ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885), clpC, SAB0475 (STAAB), mecA, ERS140147_01863 (STAAB)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CLPC_STAAB] Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. [A0A077UK83_STAAU] Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis.[HAMAP-Rule:MF_01124][SAAS:SAAS00950444]

Publication Abstract from PubMed

Ring-forming AAA+ chaperones exert ATP-fueled substrate unfolding by threading through a central pore. This activity is potentially harmful requiring mechanisms for tight repression and substrate-specific activation. The AAA+ chaperone ClpC with the peptidase ClpP forms a bacterial protease essential to virulence and stress resistance. The adaptor MecA activates ClpC by targeting substrates and stimulating ClpC ATPase activity. We show how ClpC is repressed in its ground state by determining ClpC cryo-EM structures with and without MecA. ClpC forms large two-helical assemblies that associate via head-to-head contacts between coiled-coil middle domains (MDs). MecA converts this resting state to an active planar ring structure by binding to MD interaction sites. Loss of ClpC repression in MD mutants causes constitutive activation and severe cellular toxicity. These findings unravel an unexpected regulatory concept executed by coiled-coil MDs to tightly control AAA+ chaperone activity.

Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control.,Carroni M, Franke KB, Maurer M, Jager J, Hantke I, Gloge F, Linder D, Gremer S, Turgay K, Bukau B, Mogk A Elife. 2017 Nov 22;6. doi: 10.7554/eLife.30120. PMID:29165246^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Carroni M, Franke KB, Maurer M, Jager J, Hantke I, Gloge F, Linder D, Gremer S, Turgay K, Bukau B, Mogk A. Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control. Elife. 2017 Nov 22;6. doi: 10.7554/eLife.30120. PMID:29165246 doi:http://dx.doi.org/10.7554/eLife.30120

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6emw"

@@ Line 3: / Line 3: @@
 <StructureSection load='6emw' size='340' side='right' caption='[[6emw]], [[Resolution|resolution]] 11.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6emw]] is a 42 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EMW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EMW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6emw]] is a 42 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885] and [http://en.wikipedia.org/wiki/Staab Staab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EMW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EMW FirstGlance]. <br>
-</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=6emw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6emw OCA], [http://pdbe.org/6emw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6emw RCSB], [http://www.ebi.ac.uk/pdbsum/6emw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6emw ProSAT]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA803_07045 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885]), clpC, BN1321_130009 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885]), clpC, SAB0475 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273036 STAAB]), mecA, ERS140147_01863 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273036 STAAB])</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=6emw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6emw OCA], [http://pdbe.org/6emw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6emw RCSB], [http://www.ebi.ac.uk/pdbsum/6emw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6emw ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Staab]]
 [[Category: Bukau, B]]
 [[Category: Carroni, M]]

6emw

From Proteopedia

Revision as of 06:55, 24 October 2018

Structure of S.aureus ClpC in complex with MecA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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