2k77: Difference between revisions
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< | ==NMR solution structure of the Bacillus subtilis ClpC N-domain== | ||
<StructureSection load='2k77' size='340' side='right'caption='[[2k77]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2k77]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K77 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2k77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k77 OCA], [https://pdbe.org/2k77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k77 RCSB], [https://www.ebi.ac.uk/pdbsum/2k77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k77 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. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/2k77_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2k77 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The AAA(+) (ATPases associated with a variety of cellular activities) superfamily protein ClpC is a key regulator of cell development in Bacillus subtilis. As part of a large oligomeric complex, ClpC controls an array of cellular processes by recognizing, unfolding, and providing misfolded and aggregated proteins as substrates for the ClpP peptidase. ClpC is unique compared to other HSP100/Clp proteins, as it requires an adaptor protein for all fundamental activities. The NMR solution structure of the N-terminal repeat domain of ClpC (N-ClpCR) comprises two structural repeats of a four-helix motif. NMR experiments used to map the MecA adaptor protein interaction surface of N-ClpCR reveal that regions involved in the interaction possess conformational flexibility and conformational exchange on the microsecond-to-millisecond timescale. The electrostatic surface of N-ClpCR differs substantially from the N-domain of Escherichia coli ClpA and ClpB, suggesting that the electrostatic surface characteristics of HSP100/Clp N-domains may play a role in adaptor protein and substrate interaction specificity, and perhaps contribute to the unique adaptor protein requirement of ClpC. | |||
Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions.,Kojetin DJ, McLaughlin PD, Thompson RJ, Dubnau D, Prepiak P, Rance M, Cavanagh J J Mol Biol. 2009 Apr 3;387(3):639-52. Epub 2009 Jan 30. PMID:19361434<ref>PMID:19361434</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2k77" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Cavanagh J]] | ||
[[Category: | [[Category: Kojetin DJ]] | ||
[[Category: | [[Category: McLaughlin PD]] | ||
[[Category: | [[Category: Rance M]] | ||
[[Category: | [[Category: Thompson RJ]] | ||
Latest revision as of 12:45, 9 May 2024
NMR solution structure of the Bacillus subtilis ClpC N-domainNMR solution structure of the Bacillus subtilis ClpC N-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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe AAA(+) (ATPases associated with a variety of cellular activities) superfamily protein ClpC is a key regulator of cell development in Bacillus subtilis. As part of a large oligomeric complex, ClpC controls an array of cellular processes by recognizing, unfolding, and providing misfolded and aggregated proteins as substrates for the ClpP peptidase. ClpC is unique compared to other HSP100/Clp proteins, as it requires an adaptor protein for all fundamental activities. The NMR solution structure of the N-terminal repeat domain of ClpC (N-ClpCR) comprises two structural repeats of a four-helix motif. NMR experiments used to map the MecA adaptor protein interaction surface of N-ClpCR reveal that regions involved in the interaction possess conformational flexibility and conformational exchange on the microsecond-to-millisecond timescale. The electrostatic surface of N-ClpCR differs substantially from the N-domain of Escherichia coli ClpA and ClpB, suggesting that the electrostatic surface characteristics of HSP100/Clp N-domains may play a role in adaptor protein and substrate interaction specificity, and perhaps contribute to the unique adaptor protein requirement of ClpC. Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions.,Kojetin DJ, McLaughlin PD, Thompson RJ, Dubnau D, Prepiak P, Rance M, Cavanagh J J Mol Biol. 2009 Apr 3;387(3):639-52. Epub 2009 Jan 30. PMID:19361434[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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