9dvy

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Current revision (07:05, 15 October 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9dvy is ON HOLD until Paper Publication
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==Human mitochondrial ClpX with endogenous substrate==
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<StructureSection load='9dvy' size='340' side='right'caption='[[9dvy]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9dvy]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9DVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9DVY FirstGlance]. <br>
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Description:
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=9dvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9dvy OCA], [https://pdbe.org/9dvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9dvy RCSB], [https://www.ebi.ac.uk/pdbsum/9dvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9dvy ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CLPX_HUMAN CLPX_HUMAN] The disease may be caused by variants affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/CLPX_HUMAN CLPX_HUMAN] ATP-dependent chaperone that functions as an unfoldase. As part of the ClpXP protease complex, it recognizes specific protein substrates, unfolds them using energy derived from ATP hydrolysis, and then translocates them to the proteolytic subunit (CLPP) of the ClpXP complex for degradation (PubMed:11923310, PubMed:22710082, PubMed:28874591). Thanks to its chaperone activity, it also functions in the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis (PubMed:28874591). This chaperone is also involved in the control of mtDNA nucleoid distribution, by regulating mitochondrial transcription factor A (TFAM) activity (PubMed:22841477).<ref>PMID:11923310</ref> <ref>PMID:22710082</ref> <ref>PMID:22841477</ref> <ref>PMID:28874591</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Chen WC]]

Current revision

Human mitochondrial ClpX with endogenous substrate

PDB ID 9dvy

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