4d2q

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==Negative-stain electron microscopy of E. coli ClpB mutant E432A (BAP form bound to ClpP)==
==Negative-stain electron microscopy of E. coli ClpB mutant E432A (BAP form bound to ClpP)==
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<StructureSection load='4d2q' size='340' side='right' caption='[[4d2q]], [[Resolution|resolution]] 18.00&Aring;' scene=''>
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<SX load='4d2q' size='340' side='right' viewer='molstar' caption='[[4d2q]], [[Resolution|resolution]] 18.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4d2q]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D2Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4d2q]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D2Q FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 18&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d2u|4d2u]], [[4d2x|4d2x]]</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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d2q RCSB], [http://www.ebi.ac.uk/pdbsum/4d2q PDBsum]</span></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=4d2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2q OCA], [https://pdbe.org/4d2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d2q RCSB], [https://www.ebi.ac.uk/pdbsum/4d2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d2q ProSAT]</span></td></tr>
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<table>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CLPB_ECOLI CLPB_ECOLI] Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK.<ref>PMID:10982797</ref> <ref>PMID:12624113</ref> <ref>PMID:14640692</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation.,Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, Kopp J, Mogk A, Bukau B, Saibil HR Elife. 2014 Apr 30;3:e02481. doi: 10.7554/eLife.02481. PMID:24843029<ref>PMID:24843029</ref>
Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation.,Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, Kopp J, Mogk A, Bukau B, Saibil HR Elife. 2014 Apr 30;3:e02481. doi: 10.7554/eLife.02481. PMID:24843029<ref>PMID:24843029</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4d2q" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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*[[3D structures of ClpB|3D structures of ClpB]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Bukau, B.]]
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[[Category: Escherichia coli]]
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[[Category: Carroni, M.]]
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[[Category: Large Structures]]
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[[Category: Clare, D K.]]
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[[Category: Bukau B]]
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[[Category: Kopp, J.]]
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[[Category: Carroni M]]
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[[Category: Kummer, E.]]
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[[Category: Clare DK]]
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[[Category: Mogk, A.]]
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[[Category: Kopp J]]
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[[Category: Oguchi, Y.]]
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[[Category: Kummer E]]
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[[Category: Saibil, H R.]]
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[[Category: Mogk A]]
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[[Category: Sinning, I.]]
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[[Category: Oguchi Y]]
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[[Category: Wendler, P.]]
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[[Category: Saibil HR]]
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[[Category: Bap]]
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[[Category: Sinning I]]
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[[Category: Chaperone]]
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[[Category: Wendler P]]
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[[Category: Clpb]]
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[[Category: Coiled-coil domain]]
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[[Category: Disaggregase]]
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Current revision

Negative-stain electron microscopy of E. coli ClpB mutant E432A (BAP form bound to ClpP)

4d2q, resolution 18.00Å

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