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2kqx

From Proteopedia

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[[Image:2kqx.png|left|200px]]
 
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==NMR structure of the J-domain (residues 2-72) in the Escherichia coli CbpA==
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The line below this paragraph, containing "STRUCTURE_2kqx", creates the "Structure Box" on the page.
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<StructureSection load='2kqx' size='340' side='right'caption='[[2kqx]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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{{STRUCTURE_2kqx| PDB=2kqx | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kq/2kqx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===NMR structure of the J-domain (residues 2-72) in the Escherichia coli CbpA===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20226195}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2kqx" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20226195 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20226195}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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[[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].
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[[Category: Large Structures]]
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[[Category: Ekiel I]]
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==Reference==
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<ref group="xtra">PMID:20226195</ref><references group="xtra"/>
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[[Category: Escherichia coli k-12]]
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[[Category: Ekiel, I.]]
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[[Category: Cbpa-j domain]]
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[[Category: Chaperone binding protein]]
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[[Category: Co-chaperone]]
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[[Category: Escherichia coli]]
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Current revision

NMR structure of the J-domain (residues 2-72) in the Escherichia coli CbpA

PDB ID 2kqx

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