NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.

摘要: The solution structure of the 21 kDa substrate-binding domain Escherichia coli Hsp70-chaperone protein DnaK (DnaK 386−561) has been determined to a precision 1.00 A (backbone β-domain) from 1075 experimental restraints obtained multinuclear, multidimensional NMR experiments. is observed bind its own C-terminus and offers preview interaction this chaperone with other proteins. bound region tightly held at single amino acid position (a leucyl residue) that buried in deep pocket lined conserved hydrophobic residues. second binding site was identified using paramagnetically labeled peptides. It located close N-terminus may constitute allosteric links affinity nucleotide Hsp70 chaperones.