4lj6

ClpB NBD2 from T. thermophilus in complex with AMPPCPClpB NBD2 from T. thermophilus in complex with AMPPCP

FunctionFunction

[CLPB_THET8] 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]

About this StructureAbout this Structure

4lj6 is a 1 chain structure. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ Zeymer C, Barends TR, Werbeck ND, Schlichting I, Reinstein J. Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):582-95. doi:, 10.1107/S1399004713030629. Epub 2014 Jan 31. PMID:24531492 doi:http://dx.doi.org/10.1107/S1399004713030629

↑ Motohashi K, Watanabe Y, Yohda M, Yoshida M. Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7184-9. PMID:10377389

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OCA

[2] Zeymer C, Barends TR, Werbeck ND, Schlichting I, Reinstein J. Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):582-95. doi:, 10.1107/S1399004713030629. Epub 2014 Jan 31. PMID:24531492 doi:http://dx.doi.org/10.1107/S1399004713030629

[1] Motohashi K, Watanabe Y, Yohda M, Yoshida M. Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7184-9. PMID:10377389

[1]

[xtra 1]