6og3

From Proteopedia

(Difference between revisions)

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?)

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