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| | ==Crystal structure of symmetric W-W-W ClpX Hexamer== | | ==Crystal structure of symmetric W-W-W ClpX Hexamer== |
| - | <StructureSection load='4i9k' size='340' side='right' caption='[[4i9k]], [[Resolution|resolution]] 5.00Å' scene=''> | + | <StructureSection load='4i9k' size='340' side='right'caption='[[4i9k]], [[Resolution|resolution]] 5.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4i9k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I9K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I9K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4i9k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I9K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 5.0003Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hws|3hws]], [[3hte|3hte]], [[4i4l|4i4l]], [[4i34|4i34]], [[4i5o|4i5o]], [[4i63|4i63]], [[4i81|4i81]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0438, clpX, JW0428, lopC ([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'>[https://proteopedia.org/fgij/fg.htm?mol=4i9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i9k OCA], [https://pdbe.org/4i9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i9k RCSB], [https://www.ebi.ac.uk/pdbsum/4i9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i9k ProSAT]</span></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=4i9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i9k OCA], [http://pdbe.org/4i9k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i9k RCSB], [http://www.ebi.ac.uk/pdbsum/4i9k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i9k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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] | + | [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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[ClpX|ClpX]] | + | *[[Clp protease 3D structures|Clp protease 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Baker, T A]] | + | [[Category: Large Structures]] |
| - | [[Category: Glynn, S E]] | + | [[Category: Baker TA]] |
| - | [[Category: Nager, A R]] | + | [[Category: Glynn SE]] |
| - | [[Category: Sauer, R T]] | + | [[Category: Nager AR]] |
| - | [[Category: Schmitz, K R]] | + | [[Category: Sauer RT]] |
| - | [[Category: Stinson, B S]] | + | [[Category: Schmitz KR]] |
| - | [[Category: Atpase]] | + | [[Category: Stinson BS]] |
| - | [[Category: Hexamer]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Symmetric]]
| + | |
| Structural highlights
Function
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]
Publication Abstract from PubMed
ClpX, a AAA+ ring homohexamer, uses the energy of ATP binding and hydrolysis to power conformational changes that unfold and translocate target proteins into the ClpP peptidase for degradation. In multiple crystal structures, some ClpX subunits adopt nucleotide-loadable conformations, others adopt unloadable conformations, and each conformational class exhibits substantial variability. Using mutagenesis of individual subunits in covalently tethered hexamers together with fluorescence methods to assay the conformations and nucleotide-binding properties of these subunits, we demonstrate that dynamic interconversion between loadable and unloadable conformations is required to couple ATP hydrolysis by ClpX to mechanical work. ATP binding to different classes of subunits initially drives staged allosteric changes, which set the conformation of the ring to allow hydrolysis and linked mechanical steps. Subunit switching between loadable and unloadable conformations subsequently isomerizes or resets the configuration of the nucleotide-loaded ring and is required for mechanical function.
Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine.,Stinson BM, Nager AR, Glynn SE, Schmitz KR, Baker TA, Sauer RT Cell. 2013 Apr 25;153(3):628-39. doi: 10.1016/j.cell.2013.03.029. PMID:23622246[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stinson BM, Nager AR, Glynn SE, Schmitz KR, Baker TA, Sauer RT. Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine. Cell. 2013 Apr 25;153(3):628-39. doi: 10.1016/j.cell.2013.03.029. PMID:23622246 doi:10.1016/j.cell.2013.03.029
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