1i69: Difference between revisions

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New page: left|200px<br /><applet load="1i69" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i69, resolution 2.7Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1i69.jpg|left|200px]]<br /><applet load="1i69" size="450" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTAL STRUCTURE OF THE REDUCED FORM OF OXYR'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE REDUCED FORM OF OXYR==
The Escherichia coli OxyR transcription factor senses H2O2 and is, activated through the formation of an intramolecular disulfide bond. Here, we present the crystal structures of the regulatory domain of OxyR in its, reduced and oxidized forms, determined at 2.7 A and 2.3 A resolutions, respectively. In the reduced form, the two redox-active cysteines are, separated by approximately 17 A. Disulfide bond formation in the oxidized, form results in a significant structural change in the regulatory domain., The structural remodeling, which leads to different oligomeric, associations, accounts for the redox-dependent switch in OxyR and provides, a novel example of protein regulation by "fold editing" through a, reversible disulfide bond formation within a folded domain.
<StructureSection load='1i69' size='340' side='right'caption='[[1i69]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1i69]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I69 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i69 OCA], [https://pdbe.org/1i69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i69 RCSB], [https://www.ebi.ac.uk/pdbsum/1i69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i69 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OXYR_ECOLI OXYR_ECOLI] Hydrogen peroxide sensor. Activates the expression of a regulon of hydrogen peroxide-inducible genes such as katG, gor, ahpC, ahpF, oxyS (a regulatory RNA), dps, fur and grxA. OxyR expression is negatively autoregulated by binding to a 43 bp region upstream of its own coding sequence. OxyR is inactivated by reduction of its essential disulfide bond by the product of GrxA, itself positively regulated by OxyR. Has also a positive regulatory effect on the production of surface proteins that control the colony morphology and auto-aggregation ability.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i6/1i69_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1i69 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1I69 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with BEZ as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I69 OCA].
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structural basis of the redox switch in the OxyR transcription factor., Choi H, Kim S, Mukhopadhyay P, Cho S, Woo J, Storz G, Ryu S, Cell. 2001 Apr 6;105(1):103-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11301006 11301006]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Choi, H.]]
[[Category: Choi H]]
[[Category: Kim, S.]]
[[Category: Kim S]]
[[Category: Ryu, S.]]
[[Category: Ryu S]]
[[Category: BEZ]]
[[Category: oxyr regulatory domain]]
[[Category: reduced form]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:05:04 2007''

Latest revision as of 10:32, 7 February 2024

CRYSTAL STRUCTURE OF THE REDUCED FORM OF OXYRCRYSTAL STRUCTURE OF THE REDUCED FORM OF OXYR

Structural highlights

1i69 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OXYR_ECOLI Hydrogen peroxide sensor. Activates the expression of a regulon of hydrogen peroxide-inducible genes such as katG, gor, ahpC, ahpF, oxyS (a regulatory RNA), dps, fur and grxA. OxyR expression is negatively autoregulated by binding to a 43 bp region upstream of its own coding sequence. OxyR is inactivated by reduction of its essential disulfide bond by the product of GrxA, itself positively regulated by OxyR. Has also a positive regulatory effect on the production of surface proteins that control the colony morphology and auto-aggregation ability.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1i69, resolution 2.70Å

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