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.


6oay

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:23, 20 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<SX load='6oay' size='340' side='right' viewer='molstar' caption='[[6oay]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<SX load='6oay' size='340' side='right' viewer='molstar' caption='[[6oay]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6oay]] is a 7 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=6OAY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OAY FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6oay]] is a 7 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=6OAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OAY FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</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]] 3.3&#8491;</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>
+
<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6oax|6oax]], [[6og2|6og2]], [[6og1|6og1]], [[6og3|6og3]]</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=6oay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oay OCA], [https://pdbe.org/6oay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oay RCSB], [https://www.ebi.ac.uk/pdbsum/6oay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oay 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=6oay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oay OCA], [http://pdbe.org/6oay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oay RCSB], [http://www.ebi.ac.uk/pdbsum/6oay PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oay ProSAT]</span></td></tr>
+
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[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>
-
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>
+
==See Also==
-
 
+
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
*[[3D structures of ClpB|3D structures of ClpB]]
-
</div>
+
-
<div class="pdbe-citations 6oay" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
Line 23: Line 19:
</SX>
</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]]
+

Current revision

Structure of the hyperactive ClpB mutant K476C, bound to casein, post-state

6oay, resolution 3.30Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6oay"
Personal tools