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6w22

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Current revision (14:41, 6 March 2024) (edit) (undo)
 
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<StructureSection load='6w22' size='340' side='right'caption='[[6w22]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='6w22' size='340' side='right'caption='[[6w22]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6w22]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli] and [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W22 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6W22 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6w22]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6W22 FirstGlance]. <br>
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</td></tr><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></td></tr>
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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&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
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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></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpA, lopD, b0882, JW0866 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=6w22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w22 OCA], [https://pdbe.org/6w22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w22 RCSB], [https://www.ebi.ac.uk/pdbsum/6w22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w22 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6w22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w22 OCA], [http://pdbe.org/6w22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6w22 RCSB], [http://www.ebi.ac.uk/pdbsum/6w22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6w22 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CLPA_ECOLI CLPA_ECOLI]] ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins.
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[https://www.uniprot.org/uniprot/CLPA_ECOLI CLPA_ECOLI] ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The ClpAP complex is a conserved bacterial protease that unfolds and degrades proteins targeted for destruction. The ClpA double-ring hexamer powers substrate unfolding and translocation into the ClpP proteolytic chamber. Here, we determined high-resolution structures of wild-type Escherichia coli ClpAP undergoing active substrate unfolding and proteolysis. A spiral of pore loop-substrate contacts spans both ClpA AAA+ domains. Protomers at the spiral seam undergo nucleotide-specific rearrangements, supporting substrate translocation. IGL loops extend flexibly to bind the planar, heptameric ClpP surface with the empty, symmetry-mismatched IGL pocket maintained at the seam. Three different structures identify a binding-pocket switch by the IGL loop of the lowest positioned protomer, involving release and re-engagement with the clockwise pocket. This switch is coupled to a ClpA rotation and a network of conformational changes across the seam, suggesting that ClpA can rotate around the ClpP apical surface during processive steps of translocation and proteolysis.
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Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.,Lopez KE, Rizo AN, Tse E, Lin J, Scull NW, Thwin AC, Lucius AL, Shorter J, Southworth DR Nat Struct Mol Biol. 2020 Apr 20. pii: 10.1038/s41594-020-0409-5. doi:, 10.1038/s41594-020-0409-5. PMID:32313240<ref>PMID:32313240</ref>
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==See Also==
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*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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</div>
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<div class="pdbe-citations 6w22" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Synthetic construct sequences]]
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[[Category: Synthetic construct]]
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[[Category: Lin, J]]
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[[Category: Lin J]]
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[[Category: Lopez, K L]]
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[[Category: Lopez KL]]
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[[Category: Lucius, A L]]
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[[Category: Lucius AL]]
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[[Category: Rizo, A N]]
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[[Category: Rizo AN]]
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[[Category: Scull, N W]]
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[[Category: Scull NW]]
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[[Category: Shorter, J]]
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[[Category: Shorter J]]
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[[Category: Southworth, D R]]
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[[Category: Southworth DR]]
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[[Category: Thwin, A C]]
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[[Category: Thwin AC]]
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[[Category: Tse, E]]
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[[Category: Tse E]]
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[[Category: Aaa+]]
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[[Category: Atpase]]
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[[Category: Chaperone]]
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[[Category: Hsp100]]
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[[Category: Protease]]
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Current revision

ClpA Engaged1 State bound to RepA-GFP (ClpA Focused Refinement)

PDB ID 6w22

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