6oay

Structure of the hyperactive ClpB mutant K476C, bound to casein, post-stateStructure of the hyperactive ClpB mutant K476C, bound to casein, post-state

6oay, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Structural highlights 6oay is a 7 chain structure with sequence from Bos taurus and Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.3Å Ligands: Experimental data: Check 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. See Also Heat Shock Protein structures 3D structures of ClpB