2BPR
NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, 25 STRUCTURES
Summary for 2BPR
| Entry DOI | 10.2210/pdb2bpr/pdb |
| Descriptor | DNAK (1 entity in total) |
| Functional Keywords | molecular chaperone, hsp70, peptide binding, protein folding |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm: P0A6Y8 |
| 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 Cited by 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: 9609686DOI: 10.1021/bi9800855 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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