1bpr
From Proteopedia
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NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE
Overview
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.
About this Structure
1BPR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction., Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER, Biochemistry. 1998 Jun 2;37(22):7929-40. PMID:9609686
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