1BPR

NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE

Summary for 1BPR

• Entry DOI: 10.2210/pdb1bpr/pdb
• Descriptor: DNAK (1 entity in total)
• Functional Keywords: molecular chaperone, hsp70, peptide binding, protein folding
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 20940.34

Authors

Wang, H.,Kurochkin, A.V.,Pang, Y.,Hu, W.,Flynn, G.C.,Zuiderweg, E.R.P. (deposition date: 1998-08-11, release date: 1999-03-02, Last modification date: 2024-05-22)

Primary citation

Wang, H.,Kurochkin, A.V.,Pang, Y.,Hu, W.,Flynn, G.C.,Zuiderweg, E.R.
NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.
Biochemistry, 37:7929-7940, 1998

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

PubMed: 9609686
DOI: 10.1021/bi9800855

Experimental method

SOLUTION NMR