1ovx

<StructureSection load='1ovx' size='340' side='right' caption='[[1ovx]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1ovx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OVX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Clpx ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ovx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ovx OCA], [http://pdbe.org/1ovx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ovx RCSB], [http://www.ebi.ac.uk/pdbsum/1ovx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ovx ProSAT]</span></td></tr>

[[http://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]

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== Publication Abstract from PubMed ==

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.

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:14525985<ref>PMID:14525985</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ovx" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Ecoli]]

[[Category: Donaldson, L W]]

[[Category: Houry, W A]]

[[Category: Kwan, J]]

[[Category: Wojtyra, U]]

[[Category: Homodimer]]

[[Category: Treble clef zinc finger]]