1bpr: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1bpr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BPR FirstGlance]. <br> | <table><tr><td colspan='2'>[[1bpr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BPR FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1bpr RCSB], [http://www.ebi.ac.uk/pdbsum/1bpr PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1bpr RCSB], [http://www.ebi.ac.uk/pdbsum/1bpr PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Flynn, G C | [[Category: Flynn, G C]] | ||
[[Category: Hu, W | [[Category: Hu, W]] | ||
[[Category: Kurochkin, A V | [[Category: Kurochkin, A V]] | ||
[[Category: Pang, Y | [[Category: Pang, Y]] | ||
[[Category: Wang, H | [[Category: Wang, H]] | ||
[[Category: Zuiderweg, E R.P | [[Category: Zuiderweg, E R.P]] | ||
[[Category: Hsp70]] | [[Category: Hsp70]] | ||
[[Category: Molecular chaperone]] | [[Category: Molecular chaperone]] | ||
[[Category: Peptide binding]] | [[Category: Peptide binding]] | ||
[[Category: Protein folding]] | [[Category: Protein folding]] | ||
Revision as of 12:58, 22 December 2014
NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURENMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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