This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

6og3

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

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

6og3, resolution 4.10Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6og3"

@@ Line 3: / Line 3: @@
 <SX load='6og3' size='340' side='right' viewer='molstar' caption='[[6og3]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
 == 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://proteopedia.org/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://proteopedia.org/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>
 == 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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Bacterial ClpB and yeast Hsp104 are homologous Hsp100 protein disaggregases that serve critical functions in proteostasis by solubilizing protein aggregates. Two AAA+ nucleotide binding domains (NBDs) power polypeptide translocation through a central channel comprised of a hexameric spiral of protomers that contact substrate via conserved pore-loop interactions. Here we report cryo-EM structures of a hyperactive ClpB variant bound to the model substrate, casein in the presence of slowly hydrolysable ATPgammaS, which reveal the translocation mechanism. Distinct substrate-gripping interactions are identified for NBD1 and NBD2 pore loops. A trimer of N-terminal domains define a channel entrance that binds the polypeptide substrate adjacent to the topmost NBD1 contact. NBD conformations at the seam interface reveal how ATP hydrolysis-driven substrate disengagement and re-binding are precisely tuned to drive a directional, stepwise translocation cycle.
-Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase.,Rizo AN, Lin J, Gates SN, Tse E, Bart SM, Castellano LM, DiMaio F, Shorter J, Southworth DR Nat Commun. 2019 Jun 3;10(1):2393. doi: 10.1038/s41467-019-10150-y. PMID:31160557<ref>PMID:31160557</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6og3" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Heat Shock Protein structures|Heat Shock Protein structures]]
+*[[3D structures of ClpB|3D structures of ClpB]]
 == References ==
 <references/>
@@ Line 27: / Line 18: @@
 </SX>
 [[Category: Bos taurus]]
+[[Category: Escherichia coli K-12]]
 [[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]]

6og3

From Proteopedia

Current revision

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

Structural highlights

Function

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox