4d2x

From Proteopedia

(Difference between revisions)

Revision as of 14:50, 25 December 2014

Negative-stain electron microscopy of E. coli ClpB of Y503D hyperactive mutant (BAP form bound to ClpP)

Structural highlights

4d2x is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	4d2q, 4d2u
Resources:	FirstGlance, OCA, RCSB, PDBsum

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

The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation with the Hsp70 system. Essential for disaggregation, the ClpB middle domain (MD) is a coiled-coil propeller that binds Hsp70. Although the ClpB subunit structure is known, positioning of the MD in the hexamer and its mechanism of action are unclear. We obtained electron microscopy (EM) structures of the BAP variant of ClpB that binds the protease ClpP, clearly revealing MD density on the surface of the ClpB ring. Mutant analysis and asymmetric reconstructions show that MDs adopt diverse positions in a single ClpB hexamer. Adjacent, horizontally oriented MDs form head-to-tail contacts and repress ClpB activity by preventing Hsp70 interaction. Tilting of the MD breaks this contact, allowing Hsp70 binding, and releasing the contact in adjacent subunits. Our data suggest a wavelike activation of ClpB subunits around the ring.DOI: http://dx.doi.org/10.7554/eLife.02481.001.

Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation.,Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, Kopp J, Mogk A, Bukau B, Saibil HR Elife. 2014 Apr 30;3:e02481. doi: 10.7554/eLife.02481. PMID:24843029^[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
↑ Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, Kopp J, Mogk A, Bukau B, Saibil HR. Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Elife. 2014 Apr 30;3:e02481. doi: 10.7554/eLife.02481. PMID:24843029

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4d2x"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4d2x]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D2X FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d2q|4d2q]], [[4d2u|4d2u]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d2q|4d2q]], [[4d2u|4d2u]]</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d2x RCSB], [http://www.ebi.ac.uk/pdbsum/4d2x PDBsum]</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=4d2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d2x RCSB], [http://www.ebi.ac.uk/pdbsum/4d2x PDBsum]</span></td></tr>
-<table>
+</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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 13: / Line 15: @@
 Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation.,Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, Kopp J, Mogk A, Bukau B, Saibil HR Elife. 2014 Apr 30;3:e02481. doi: 10.7554/eLife.02481. PMID:24843029<ref>PMID:24843029</ref>
-From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
 == References ==
@@ Line 19: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Bukau, B.]]
+[[Category: Bukau, B]]
-[[Category: Carroni, M.]]
+[[Category: Carroni, M]]
-[[Category: Clare, D K.]]
+[[Category: Clare, D K]]
-[[Category: Kopp, J.]]
+[[Category: Kopp, J]]
-[[Category: Kummer, E.]]
+[[Category: Kummer, E]]
-[[Category: Mogk, A.]]
+[[Category: Mogk, A]]
-[[Category: Oguchi, Y.]]
+[[Category: Oguchi, Y]]
-[[Category: Saibil, H R.]]
+[[Category: Saibil, H R]]
-[[Category: Sinning, I.]]
+[[Category: Sinning, I]]
-[[Category: Wendler, P.]]
+[[Category: Wendler, P]]
 [[Category: Bap]]
 [[Category: Chaperone]]

4d2x

From Proteopedia

Revision as of 14:50, 25 December 2014

Negative-stain electron microscopy of E. coli ClpB of Y503D hyperactive mutant (BAP form bound to ClpP)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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