1bpr

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bpr OCA], [http://www.ebi.ac.uk/pdbsum/1bpr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bpr RCSB]</span>
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'''NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE'''
'''NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE'''
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[[Category: Wang, H.]]
[[Category: Wang, H.]]
[[Category: Zuiderweg, E R.P.]]
[[Category: Zuiderweg, E R.P.]]
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[[Category: hsp70]]
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[[Category: Hsp70]]
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[[Category: molecular chaperone]]
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[[Category: Molecular chaperone]]
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[[Category: peptide binding]]
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[[Category: Peptide binding]]
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[[Category: protein folding]]
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[[Category: Protein folding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:48:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:05:46 2008''
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Revision as of 08:48, 2 May 2008

Template:STRUCTURE 1bpr

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 Page seeded by OCA on Fri May 2 11:48:19 2008

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