1bpr
From Proteopedia
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| - | [[Image:1bpr.gif|left|200px]] | + | [[Image:1bpr.gif|left|200px]] |
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| - | '''NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE''' | + | {{Structure |
| + | |PDB= 1bpr |SIZE=350|CAPTION= <scene name='initialview01'>1bpr</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BPR is a [ | + | 1BPR is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9609686 9609686] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein folding]] | [[Category: protein folding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:14:08 2008'' |
Revision as of 08:14, 20 March 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 Mar 20 10:14:08 2008
