6w6g
From Proteopedia
(Difference between revisions)
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- | ==== | + | ==The Mycobacterium tuberculosis ClpB disaggregase hexamer structure in conformation I in the presence of DnaK chaperone and a model substrate== |
- | <StructureSection load='6w6g' size='340' side='right'caption='[[6w6g]]' scene=''> | + | <StructureSection load='6w6g' size='340' side='right'caption='[[6w6g]], [[Resolution|resolution]] 3.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6w6g]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6W6G FirstGlance]. <br> |
- | </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=6w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w6g OCA], [https://pdbe.org/6w6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w6g RCSB], [https://www.ebi.ac.uk/pdbsum/6w6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w6g ProSAT]</span></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]] 3.1Å</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=6w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w6g OCA], [https://pdbe.org/6w6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w6g RCSB], [https://www.ebi.ac.uk/pdbsum/6w6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w6g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/CLPB_MYCTU CLPB_MYCTU] 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 (By similarity). | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The M. tuberculosis (Mtb) ClpB is a protein disaggregase that helps to rejuvenate the bacterial cell. DnaK is a protein foldase that can function alone, but it can also bind to the ClpB hexamer to physically couple protein disaggregation with protein refolding, although the molecular mechanism is not well understood. Here, we report the cryo-EM analysis of the Mtb ClpB-DnaK bi-chaperone in the presence of ATPgammaS and a protein substrate. We observe three ClpB conformations in the presence of DnaK, identify a conserved TGIP loop linking the oligonucleotide/oligosaccharide-binding domain and the nucleotide-binding domain that is important for ClpB function, derive the interface between the regulatory middle domain of the ClpB and the DnaK nucleotide-binding domain, and find that DnaK binding stabilizes, but does not bend or tilt, the ClpB middle domain. We propose a model for the synergistic actions of aggregate dissolution and refolding by the Mtb ClpB-DnaK bi-chaperone system. | ||
+ | |||
+ | Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.,Yin Y, Feng X, Yu H, Fay A, Kovach A, Glickman MS, Li H Cell Rep. 2021 May 25;35(8):109166. doi: 10.1016/j.celrep.2021.109166. PMID:34038719<ref>PMID:34038719</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6w6g" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[3D structures of ClpB|3D structures of ClpB]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Mycobacterium tuberculosis]] |
+ | [[Category: Li H]] | ||
+ | [[Category: Yin Y]] |
Current revision
The Mycobacterium tuberculosis ClpB disaggregase hexamer structure in conformation I in the presence of DnaK chaperone and a model substrate
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