6oax: Difference between revisions

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'''Unreleased structure'''


The entry 6oax is ON HOLD  until Paper Publication
==Structure of the hyperactive ClpB mutant K476C, bound to casein, pre-state==
<SX load='6oax' size='340' side='right' viewer='molstar' caption='[[6oax]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6oax]] 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=6OAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OAX 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]] 2.9&#8491;</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=6oax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oax OCA], [https://pdbe.org/6oax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oax RCSB], [https://www.ebi.ac.uk/pdbsum/6oax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oax 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>


Authors:  
==See Also==
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
Description:  
*[[3D structures of ClpB|3D structures of ClpB]]
[[Category: Unreleased Structures]]
== 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 09:23, 20 March 2024

Structure of the hyperactive ClpB mutant K476C, bound to casein, pre-state

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