1bpr
From Proteopedia
(New page: 200px<br /><applet load="1bpr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bpr" /> '''NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAI...) |
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'''NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE'''<br /> | '''NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure of the 21 kDa substrate-binding domain of the | + | 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== | ==About this Structure== | ||
| - | 1BPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1BPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BPR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Flynn, G | + | [[Category: Flynn, G C.]] |
[[Category: Hu, W.]] | [[Category: Hu, W.]] | ||
| - | [[Category: Kurochkin, A | + | [[Category: Kurochkin, A V.]] |
[[Category: Pang, Y.]] | [[Category: Pang, Y.]] | ||
[[Category: Wang, H.]] | [[Category: Wang, H.]] | ||
| - | [[Category: Zuiderweg, E | + | [[Category: Zuiderweg, E R.P.]] |
[[Category: hsp70]] | [[Category: hsp70]] | ||
[[Category: molecular chaperone]] | [[Category: molecular chaperone]] | ||
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[[Category: protein folding]] | [[Category: protein folding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:45 2008'' |
Revision as of 09:57, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 11:57:45 2008
