1q5l: Difference between revisions

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[[Image:1q5l.jpg|left|200px]]
{{Seed}}
[[Image:1q5l.png|left|200px]]


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{{STRUCTURE_1q5l|  PDB=1q5l  |  SCENE=  }}  
{{STRUCTURE_1q5l|  PDB=1q5l  |  SCENE=  }}  


'''NMR structure of the substrate binding domain of DnaK bound to the peptide NRLLLTG'''
===NMR structure of the substrate binding domain of DnaK bound to the peptide NRLLLTG===




==Overview==
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The Hsp70 family of molecular chaperones participates in a number of cellular processes, including binding to nascent polypeptide chains and assistance in protein (re)folding and degradation. We present the solution structure of the substrate binding domain (residues 393-507) of the Escherichia coli Hsp70, DnaK, that is bound to the peptide NRLLLTG and compare it to the crystal structure of DnaK(389-607) bound to the same peptide. The construct discussed here does not contain the alpha-helical domain that characterizes earlier published peptide-bound structures of the Hsp70s. It is established that removing the alpha-helical domain in its entirety does not affect the primary interactions or structure of the DnaK(393-507) in complex with the peptide NRLLLTG. In particular, the arch that protects the substrate-binding cleft is also formed in the absence of the helical lid. 15N-relaxation measurements show that the peptide-bound form of DnaK(393-507) is relatively rigid. As compared to the peptide-free state, the peptide-bound state of the domain shows distinct, widespread, and contiguous differences in structure extending toward areas previously defined as important to the allosteric regulation of the Hsp70 chaperones.
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{{ABSTRACT_PUBMED_14573869}}


==About this Structure==
==About this Structure==
1Q5L 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=1Q5L OCA].  
1Q5L is a [[Single protein]] structure of 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=1Q5L OCA].  


==Reference==
==Reference==
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[[Category: Heat shock protein]]
[[Category: Heat shock protein]]
[[Category: Hsp70]]
[[Category: Hsp70]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:53:26 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:35:51 2008''

Revision as of 08:35, 28 July 2008

File:1q5l.png

Template:STRUCTURE 1q5l

NMR structure of the substrate binding domain of DnaK bound to the peptide NRLLLTG

Template:ABSTRACT PUBMED 14573869

About this Structure

1Q5L is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG., Stevens SY, Cai S, Pellecchia M, Zuiderweg ER, Protein Sci. 2003 Nov;12(11):2588-96. PMID:14573869

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