1qw1

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[[Image:1qw1.gif|left|200px]]
 
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==Solution Structure of the C-Terminal Domain of DtxR residues 110-226==
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The line below this paragraph, containing "STRUCTURE_1qw1", creates the "Structure Box" on the page.
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<StructureSection load='1qw1' size='340' side='right'caption='[[1qw1]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qw1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QW1 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qw1 OCA], [https://pdbe.org/1qw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qw1 RCSB], [https://www.ebi.ac.uk/pdbsum/1qw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qw1 ProSAT]</span></td></tr>
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{{STRUCTURE_1qw1| PDB=1qw1 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DTXR_CORDI DTXR_CORDI] Iron-binding repressor of the dipheteria toxin gene expression. May serve as a global regulator of gene expression. Represses ripA under iron excess.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qw/1qw1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qw1 ConSurf].
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<div style="clear:both"></div>
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'''Solution Structure of the C-Terminal Domain of DtxR residues 110-226'''
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==See Also==
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*[[Diphtheria toxin repressor|Diphtheria toxin repressor]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1QW1 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=1QW1 OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15628844 15628844]
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[[Category: Corynebacterium diphtheriae]]
[[Category: Corynebacterium diphtheriae]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bienkiewicz, E A.]]
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[[Category: Bienkiewicz EA]]
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[[Category: Logan, T M.]]
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[[Category: Logan TM]]
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[[Category: Love, J F.]]
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[[Category: Love JF]]
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[[Category: Murphy, J R.]]
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[[Category: Murphy JR]]
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[[Category: Rangachari, V.]]
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[[Category: Rangachari V]]
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[[Category: Wylie, G P.]]
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[[Category: Wylie GP]]
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[[Category: C-terminal domain]]
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[[Category: Dtxr]]
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[[Category: Gene regulation]]
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[[Category: Peptide-binding]]
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[[Category: Prokaryotic sh3 domain]]
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[[Category: Repressor]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:45:50 2008''
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Current revision

Solution Structure of the C-Terminal Domain of DtxR residues 110-226

PDB ID 1qw1

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