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[[Image:2kqx.png|left|200px]]


{{STRUCTURE_2kqx| PDB=2kqx | SCENE= }}
==NMR structure of the J-domain (residues 2-72) in the Escherichia coli CbpA==
<StructureSection load='2kqx' size='340' side='right'caption='[[2kqx]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2kqx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KQX 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=2kqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kqx OCA], [https://pdbe.org/2kqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kqx RCSB], [https://www.ebi.ac.uk/pdbsum/2kqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kqx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CBPA_ECOLI CBPA_ECOLI] DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.<ref>PMID:7601860</ref> <ref>PMID:8824642</ref>
== 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/kq/2kqx_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=2kqx ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CbpA, one of the Escherichia coli DnaJ homologues, acts as a co-chaperone in the DnaK chaperone system. Despite its extensive similarity in domain structure and function to DnaJ, CbpA has a unique and specific regulatory mechanism mediated through the small protein CbpM. Both CbpA and CbpM are highly conserved in bacteria. Earlier studies showed that CbpM interacts with the N-terminal J-domain of CbpA inhibiting its co-chaperone activity but the structural basis of this interaction is not known. Here, we have combined NMR spectroscopy, site-directed mutagenesis and surface plasmon resonance to characterize the CbpA/CbpM interaction at the molecular level. We have determined the solution structure of the CbpA J-domain and mapped the residues that are perturbed upon CbpM binding. The NMR data defined a broad region on helices alpha2 and alpha 3 as involved in the interactions. Site-directed mutagenesis has been used to further delineate the CbpA J-domain/CbpM interface. We show that the binding sites of CbpM and DnaK on CbpA J-domain overlap, which suggests a competition between DnaK and CbpM for binding to CbpA as a mechanism for CbpA regulation. This study also provides the explanation for the specificity of CbpM for CbpA versus DnaJ, by identifying the key residues for differential binding.


===NMR structure of the J-domain (residues 2-72) in the Escherichia coli CbpA===
Structural basis of the regulation of the CbpA co-chaperone by its specific modulator CbpM.,Sarraf NS, Baardsnes J, Cheng J, O'Connor-McCourt M, Cygler M, Ekiel I J Mol Biol. 2010 Apr 23;398(1):111-21. Epub 2010 Mar 10. PMID:20226195<ref>PMID:20226195</ref>


{{ABSTRACT_PUBMED_20226195}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2kqx" style="background-color:#fffaf0;"></div>
[[2kqx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KQX OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:020226195</ref><references group="xtra"/>
</StructureSection>
[[Category: Escherichia coli k-12]]
[[Category: Escherichia coli K-12]]
[[Category: Ekiel, I.]]
[[Category: Large Structures]]
[[Category: Cbpa-j domain]]
[[Category: Ekiel I]]
[[Category: Chaperone binding protein]]
[[Category: Co-chaperone]]
[[Category: Escherichia coli]]
Retrieved from "https://proteopedia.org/2kqx"