1qvp: Difference between revisions

Revision as of 02:01, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1qvp.png

Template:STRUCTURE 1qvp

C terminal SH3-like domain from Diphtheria toxin Repressor residues 144-226.C terminal SH3-like domain from Diphtheria toxin Repressor residues 144-226.

Template:ABSTRACT PUBMED 15628844

About this StructureAbout this Structure

1QVP is a Single protein structure of sequence from Corynebacterium diphtheriae. Full experimental information is available from OCA.

ReferenceReference

Prolylpeptide binding by the prokaryotic SH3-like domain of the diphtheria toxin repressor: a regulatory switch., Wylie GP, Rangachari V, Bienkiewicz EA, Marin V, Bhattacharya N, Love JF, Murphy JR, Logan TM, Biochemistry. 2005 Jan 11;44(1):40-51. PMID:15628844

Page seeded by OCA on Mon Jul 28 02:01:41 2008

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

OCA

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 {{STRUCTURE_1qvp|  PDB=1qvp  |  SCENE=  }}
-'''C terminal SH3-like domain from Diphtheria toxin Repressor residues 144-226.'''
+===C terminal SH3-like domain from Diphtheria toxin Repressor residues 144-226.===
-==Overview==
+<!--
-Diphtheria toxin repressor (DtxR) regulates the expression of iron-sensitive genes in Corynebacterium diphtheriae, including the diphtheria toxin gene. DtxR contains an N-terminal metal- and DNA-binding domain that is connected by a proline-rich flexible peptide segment (Pr) to a C-terminal src homology 3 (SH3)-like domain. We determined the solution structure of the intramolecular complex formed between the proline-rich segment and the SH3-like domain by use of NMR spectroscopy. The structure of the intramolecularly bound Pr segment differs from that seen in eukaryotic prolylpeptide-SH3 domain complexes. The prolylpeptide ligand is bound by the SH3-like domain in a deep crevice lined by aliphatic amino acid residues and passes through the binding site twice but does not adopt a polyprolyl type-II helix. NMR studies indicate that this intramolecular complex is present in the apo-state of the repressor. Isothermal equilibrium denaturation studies show that intramolecular complex formation contributes to the stability of the apo-repressor. The binding affinity of synthetic peptides to the SH3-like domain was determined using isothermal titration calorimetry. From the structure and the binding energies, we calculated the enhancement in binding energy for the intramolecular reaction and compared it to the energetics of dimerization. Together, the structural and biophysical studies suggest that the proline-rich peptide segment of DtxR functions as a switch that modulates the activation of repressor activity.
+The line below this paragraph, {{ABSTRACT_PUBMED_15628844}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15628844 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15628844}}
 ==About this Structure==
-QVP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVP OCA].
+QVP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVP OCA].
 ==Reference==
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 [[Category: Repressor]]
 [[Category: Transcription regulation]]
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