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6qs7

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Revision as of 23:53, 6 March 2020

ClpB (DWB and K476C mutant) bound to casein in presence of ATPgammaS - state KC-2A

6qs7, resolution 3.80Å

Structural highlights

6qs7 is a 7 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895 and Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	clpB, htpM, b2592, JW2573 ("Bacillus coli" Migula 1895)
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

AAA+ proteins form asymmetric hexameric rings that hydrolyze ATP and thread substrate proteins through a central channel via mobile substrate-binding pore loops. Understanding how ATPase and threading activities are regulated and intertwined is key to understanding the AAA+ protein mechanism. We studied the disaggregase ClpB, which contains tandem ATPase domains (AAA1, AAA2) and shifts between low and high ATPase and threading activities. Coiled-coil M-domains repress ClpB activity by encircling the AAA1 ring. Here, we determine the mechanism of ClpB activation by comparing ATPase mechanisms and cryo-EM structures of ClpB wild-type and a constitutively active ClpB M-domain mutant. We show that ClpB activation reduces ATPase cooperativity and induces a sequential mode of ATP hydrolysis in the AAA2 ring, the main ATPase motor. AAA1 and AAA2 rings do not work synchronously but in alternating cycles. This ensures high grip, enabling substrate threading via a processive, rope-climbing mechanism.

Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor.,Deville C, Franke K, Mogk A, Bukau B, Saibil HR Cell Rep. 2019 Jun 18;27(12):3433-3446.e4. doi: 10.1016/j.celrep.2019.05.075. PMID:31216466^[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
↑ Deville C, Franke K, Mogk A, Bukau B, Saibil HR. Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor. Cell Rep. 2019 Jun 18;27(12):3433-3446.e4. doi: 10.1016/j.celrep.2019.05.075. PMID:31216466 doi:http://dx.doi.org/10.1016/j.celrep.2019.05.075

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/6qs7"

@@ Line 1: / Line 1: @@
 ==ClpB (DWB and K476C mutant) bound to casein in presence of ATPgammaS - state KC-2A==
-<StructureSection load='6qs7' size='340' side='right'caption='[[6qs7]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
+<SX load='6qs7' size='340' side='right' viewer='molstar' caption='[[6qs7]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6qs7]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] 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=6QS7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QS7 FirstGlance]. <br>
@@ Line 26: / Line 26: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Bacillus coli migula 1895]]
 [[Category: Bos taurus]]

6qs7

From Proteopedia

Revision as of 23:53, 6 March 2020

ClpB (DWB and K476C mutant) bound to casein in presence of ATPgammaS - state KC-2A

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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