1q5l: Difference between revisions

Revision as of 15:36, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 14:36:06 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1q5l.jpg|left|200px]]<br /><applet load="1q5l" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1q5l.jpg|left|200px]]<br /><applet load="1q5l" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1q5l" />
 '''NMR structure of the substrate binding domain of DnaK bound to the peptide NRLLLTG'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-Q5L 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q5L OCA].
+Q5L 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=1Q5L OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Cai, S.]]
 [[Category: Pellecchia, M.]]
-[[Category: Stevens, S.Y.]]
+[[Category: Stevens, S Y.]]
-[[Category: Zuiderweg, E.R.]]
+[[Category: Zuiderweg, E R.]]
 [[Category: chaperone]]
 [[Category: heat shock protein]]
 [[Category: hsp70]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:24:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:06 2008''