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==Structure of the hyperactive ClpB mutant K476C, bound to casein, post-state== | |||
<SX load='6oay' size='340' side='right' viewer='molstar' caption='[[6oay]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6oay]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [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=6OAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OAY FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3Å</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=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene></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=6oay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oay OCA], [https://pdbe.org/6oay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oay RCSB], [https://www.ebi.ac.uk/pdbsum/6oay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oay ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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> | |||
==See Also== | |||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | |||
*[[3D structures of ClpB|3D structures of ClpB]] | |||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</SX> | |||
[[Category: Bos taurus]] | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Bart SM]] | |||
[[Category: Castellano LM]] | |||
[[Category: Dimaio F]] | |||
[[Category: Gates SN]] | |||
[[Category: Lin J-B]] | |||
[[Category: Rizo AR]] | |||
[[Category: Shorter J]] | |||
[[Category: Southworth DR]] | |||
[[Category: Tse E]] | |||
Latest revision as of 12:23, 20 March 2024
Structure of the hyperactive ClpB mutant K476C, bound to casein, post-stateStructure of the hyperactive ClpB mutant K476C, bound to casein, post-state
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