PMID:9609686
| Citation |
Wang, H, Kurochkin, AV, Pang, Y, Hu, W, Flynn, GC and Zuiderweg, ER (1998) NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction. Biochemistry 37:7929-40 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1021/bi9800855 |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Computer Simulation; Crystallization; Escherichia coli Proteins; HSP70 Heat-Shock Proteins/chemistry; HSP70 Heat-Shock Proteins/metabolism; Humans; Models, Molecular; Molecular Chaperones/chemistry; Molecular Chaperones/metabolism; Molecular Sequence Data; Molecular Weight; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments/metabolism; Protein Structure, Tertiary; Solutions; Substrate Specificity |
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