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

Revision as of 03:57, 11 April 2020

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

6og3, resolution 4.10Å

Structural highlights

6og3 is a 4 chain structure with sequence from [1] and Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	6og1, 6og2, 6oax, 6oay
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Barnett ME, Zolkiewska A, Zolkiewski M. Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains. J Biol Chem. 2000 Dec 1;275(48):37565-71. PMID:10982797 doi:http://dx.doi.org/10.1074/jbc.M005211200
↑ Mogk A, Schlieker C, Strub C, Rist W, Weibezahn J, Bukau B. Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity. J Biol Chem. 2003 May 16;278(20):17615-24. Epub 2003 Mar 6. PMID:12624113 doi:http://dx.doi.org/10.1074/jbc.M209686200
↑ Kedzierska S, Akoev V, Barnett ME, Zolkiewski M. Structure and function of the middle domain of ClpB from Escherichia coli. Biochemistry. 2003 Dec 9;42(48):14242-8. PMID:14640692 doi:http://dx.doi.org/10.1021/bi035573d
↑ Rizo AN, Lin J, Gates SN, Tse E, Bart SM, Castellano LM, DiMaio F, Shorter J, Southworth DR. Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase. Nat Commun. 2019 Jun 3;10(1):2393. doi: 10.1038/s41467-019-10150-y. PMID:31160557 doi:http://dx.doi.org/10.1038/s41467-019-10150-y

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OG3 FirstGlance]. <br>
+<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>
 </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='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'>[http://oca.weizmann.ac.il/oca-docs/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>
+<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 ==

6og3

From Proteopedia

Revision as of 03:57, 11 April 2020

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox