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New page: left|200px<br /><applet load="1ovx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ovx" /> '''NMR structure of the E. coli ClpX chaperone ...
 
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[[Image:1ovx.jpg|left|200px]]<br /><applet load="1ovx" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ovx" />
'''NMR structure of the E. coli ClpX chaperone zinc binding domain dimer'''<br />


==Overview==
==NMR structure of the E. coli ClpX chaperone zinc binding domain dimer==
ClpX (423 amino acids), a member of the Clp/Hsp100 family of molecular, chaperones and the protease, ClpP, comprise a multimeric complex, supporting targeted protein degradation in Escherichia coli. The ClpX, sequence consists of an NH2-terminal zinc binding domain (ZBD) and a, COOH-terminal ATPase domain. Earlier, we have demonstrated that the zinc, binding domain forms a constitutive dimer that is essential for the, degradation of some ClpX substrates such as gammaO and MuA but is not, required for the degradation of other substrates such as green fluorescent, protein-SsrA. In this report, we present the NMR solution structure of the, zinc binding domain dimer. The monomer fold reveals that ZBD is a member, of the treble clef zinc finger family, a motif known to facilitate, protein-ligand, protein-DNA, and protein-protein interactions. However, the dimeric ZBD structure is not related to any protein structure in the, Protein Data Bank. A trimer-of-dimers model of ZBD is presented, which, might reflect the closed state of the ClpX hexamer.
<StructureSection load='1ovx' size='340' side='right'caption='[[1ovx]]' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1ovx]] is a 2 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=1OVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OVX FirstGlance]. <br>
1OVX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OVX OCA].  
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ovx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ovx OCA], [https://pdbe.org/1ovx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ovx RCSB], [https://www.ebi.ac.uk/pdbsum/1ovx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ovx ProSAT]</span></td></tr>
Solution structure of the dimeric zinc binding domain of the chaperone ClpX., Donaldson LW, Wojtyra U, Houry WA, J Biol Chem. 2003 Dec 5;278(49):48991-6. Epub 2003 Oct 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14525985 14525985]
</table>
[[Category: Escherichia coli]]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/CLPX_ECOLI CLPX_ECOLI] ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized and readily hydrolyzed by ClpP. Can perform chaperone functions in the absence of ClpP.[HAMAP-Rule:MF_00175]
[[Category: Donaldson, L.W.]]
== Evolutionary Conservation ==
[[Category: Houry, W.A.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Kwan, J.]]
Check<jmol>
[[Category: Wojtyra, U.]]
  <jmolCheckbox>
[[Category: ZN]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ov/1ovx_consurf.spt"</scriptWhenChecked>
[[Category: homodimer]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: treble clef zinc finger]]
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:14:25 2007''
</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=1ovx ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Donaldson LW]]
[[Category: Houry WA]]
[[Category: Kwan J]]
[[Category: Wojtyra U]]

Latest revision as of 05:51, 17 April 2024

NMR structure of the E. coli ClpX chaperone zinc binding domain dimer

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