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4lj9

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==ClpB NBD2 R621Q from T. thermophilus in complex with AMPPCP==
==ClpB NBD2 R621Q from T. thermophilus in complex with AMPPCP==
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<StructureSection load='4lj9' size='340' side='right' caption='[[4lj9]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='4lj9' size='340' side='right'caption='[[4lj9]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4lj9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LJ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LJ9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4lj9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LJ9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lj4|4lj4]], [[4lj5|4lj5]], [[4lj6|4lj6]], [[4lj7|4lj7]], [[4lj8|4lj8]], [[4lja|4lja]]</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=4lj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lj9 OCA], [https://pdbe.org/4lj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lj9 RCSB], [https://www.ebi.ac.uk/pdbsum/4lj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lj9 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</td></tr>
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<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=4lj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lj9 OCA], [http://pdbe.org/4lj9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lj9 RCSB], [http://www.ebi.ac.uk/pdbsum/4lj9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lj9 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CLPB_THET8 CLPB_THET8]] 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:10377389</ref>
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[https://www.uniprot.org/uniprot/CLPB_THET8 CLPB_THET8] 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:10377389</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4lj9" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4lj9" 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__
</StructureSection>
</StructureSection>
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[[Category: Thet8]]
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[[Category: Large Structures]]
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[[Category: Barends, T R.M]]
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[[Category: Thermus thermophilus HB8]]
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[[Category: Reinstein, J]]
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[[Category: Barends TRM]]
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[[Category: Schlichting, I]]
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[[Category: Reinstein J]]
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[[Category: Werbeck, N D]]
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[[Category: Schlichting I]]
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[[Category: Zeymer, C]]
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[[Category: Werbeck ND]]
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[[Category: Aaa+ protein]]
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[[Category: Zeymer C]]
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[[Category: Chaperone]]
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[[Category: Disaggregase]]
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[[Category: Molecular chaperone]]
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[[Category: Nucleotide binding domain]]
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Revision as of 11:04, 14 December 2022

ClpB NBD2 R621Q from T. thermophilus in complex with AMPPCP

PDB ID 4lj9

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