4hse

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Template:STRUCTURE 4hse

Contents 1 Crystal structure of ClpB NBD1 in complex with guanidinium chloride and ADP 2 Function 3 About this Structure 4 Reference

Crystal structure of ClpB NBD1 in complex with guanidinium chloride and ADP

Template:ABSTRACT PUBMED 23341453

Function

[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 Structure

4hse is a 1 chain structure with sequence from Thermus thermophilus hb8. Full crystallographic information is available from OCA.

Reference

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