6og3: Difference between revisions

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==Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, NTD-trimer==
==Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, NTD-trimer==
<StructureSection load='6og3' size='340' side='right'caption='[[6og3]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
<SX load='6og3' size='340' side='right' viewer='molstar' caption='[[6og3]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6og3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OG3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6og3]] is a 4 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=6OG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OG3 FirstGlance]. <br>
</td></tr><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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6og1|6og1]], [[6og2|6og2]], [[6oax|6oax]], [[6oay|6oay]]</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=6og3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6og3 OCA], [https://pdbe.org/6og3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6og3 RCSB], [https://www.ebi.ac.uk/pdbsum/6og3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6og3 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=6og3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6og3 OCA], [http://pdbe.org/6og3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6og3 RCSB], [http://www.ebi.ac.uk/pdbsum/6og3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6og3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bart, S M]]
[[Category: Bart SM]]
[[Category: Castellano, L M]]
[[Category: Castellano LM]]
[[Category: Dimaio, F]]
[[Category: Dimaio F]]
[[Category: Gates, S N]]
[[Category: Gates SN]]
[[Category: Lin, J B]]
[[Category: Lin J-B]]
[[Category: Rizo, A R]]
[[Category: Rizo AR]]
[[Category: Shorter, J]]
[[Category: Shorter J]]
[[Category: Southworth, D R]]
[[Category: Southworth DR]]
[[Category: Tse, E]]
[[Category: Tse E]]
[[Category: Aaa+]]
[[Category: Chaperone]]
[[Category: Clpb]]
[[Category: Disaggregase]]

Latest revision as of 12:24, 20 March 2024

Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, NTD-trimerFocus classification structure of the hyperactive ClpB mutant K476C, bound to casein, NTD-trimer

6og3, resolution 4.10Å

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