4lj4
From Proteopedia
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| - | {{STRUCTURE_4lj4| PDB=4lj4 | SCENE= }} | ||
| - | ===ClpB NBD2 from T. thermophilus, nucleotide-free=== | ||
| - | {{ABSTRACT_PUBMED_24531492}} | ||
| - | == | + | ==ClpB NBD2 from T. thermophilus, nucleotide-free== |
| - | [[http://www.uniprot.org/uniprot/CLPB_THET8 CLPB_THET8 | + | <StructureSection load='4lj4' size='340' side='right'caption='[[4lj4]], [[Resolution|resolution]] 2.80Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4lj4]] 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=4LJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LJ4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4lj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lj4 OCA], [https://pdbe.org/4lj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lj4 RCSB], [https://www.ebi.ac.uk/pdbsum/4lj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lj4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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> | ||
| - | == | + | ==See Also== |
| - | [[ | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
| - | + | *[[3D structures of ClpB|3D structures of ClpB]] | |
| - | == | + | == References == |
| - | + | <references/> | |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: | + | [[Category: Barends TRM]] |
| - | [[Category: | + | [[Category: Reinstein J]] |
| - | [[Category: | + | [[Category: Schlichting I]] |
| - | + | [[Category: Werbeck ND]] | |
| - | + | [[Category: Zeymer C]] | |
| - | + | ||
Current revision
ClpB NBD2 from T. thermophilus, nucleotide-free
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