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New page: left|200px<br /><applet load="1k6k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k6k, resolution 1.8Å" /> '''Crystal Structure of ...
 
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[[Image:1k6k.jpg|left|200px]]<br /><applet load="1k6k" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1k6k, resolution 1.8&Aring;" />
'''Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of ClpAP protease implication to the functional difference of two ATPase domains'''<br />


==Overview==
==Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of ClpAP protease implication to the functional difference of two ATPase domains==
Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component, of the ATP-dependent ClpAP protease, participates in regulatory protein, degradation and the dissolution and degradation of protein aggregates. The, crystal structure of the ClpA subunit reveals an N-terminal domain with, pseudo-twofold symmetry and two AAA(+) modules (D1 and D2) each consisting, of a large and a small sub-domain with ADP bound in the sub-domain, junction. The N-terminal domain interacts with the D1 domain in a manner, similar to adaptor-binding domains of other AAA(+) proteins. D1 and D2 are, connected head-to-tail consistent with a cooperative and vectorial, translocation of protein substrates. In a planar hexamer model of ClpA, built by assembling ClpA D1 and D2 into homohexameric rings of known, structures of AAA(+) modules, the differences in D1-D1 and D2-D2, interfaces correlate with their respective contributions to hexamer, stability and ATPase activity.
<StructureSection load='1k6k' size='340' side='right'caption='[[1k6k]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1k6k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K6K FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=1k6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k6k OCA], [https://pdbe.org/1k6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k6k RCSB], [https://www.ebi.ac.uk/pdbsum/1k6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k6k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CLPA_ECOLI CLPA_ECOLI] ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins.
== 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/k6/1k6k_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=1k6k ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1K6K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K6K OCA].
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease., Guo F, Maurizi MR, Esser L, Xia D, J Biol Chem. 2002 Nov 29;277(48):46743-52. Epub 2002 Aug 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12205096 12205096]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Esser, L.]]
[[Category: Esser L]]
[[Category: Guo, F.]]
[[Category: Guo F]]
[[Category: Maurizi, M.R.]]
[[Category: Maurizi MR]]
[[Category: Xia, D.]]
[[Category: Xia D]]
[[Category: adaptor binding]]
[[Category: atpase]]
[[Category: chaperone]]
[[Category: clpa]]
[[Category: n-domain]]
[[Category: structure]]
[[Category: x-ray]]
 
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