2zhg: Difference between revisions
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New page: left|200px {{Structure |PDB= 2zhg |SIZE=350|CAPTION= <scene name='initialview01'>2zhg</scene>, resolution 2.80Å |SITE= <scene name='pdbsite=AC1:Fes+Binding+Site+... |
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==Crystal structure of SoxR in complex with DNA== | |||
<StructureSection load='2zhg' size='340' side='right'caption='[[2zhg]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2zhg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZHG 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]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2zhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zhg OCA], [https://pdbe.org/2zhg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zhg RCSB], [https://www.ebi.ac.uk/pdbsum/2zhg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zhg ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SOXR_ECOLI SOXR_ECOLI] Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron-sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress. Upon reduction of 2Fe-2S cluster, SoxR reversibly loses its transcriptional activity, but retains its DNA binding affinity. | |||
== 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/zh/2zhg_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=2zhg ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
__TOC__ | |||
== | </StructureSection> | ||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Kita A]] | |||
[[Category: Kobayashi K]] | |||
[[Category: Miki K]] | |||
[[Category: Watanabe S]] | |||
[[Category: | |||
[[Category: Kita | |||
[[Category: Kobayashi | |||
[[Category: Miki | |||
[[Category: Watanabe | |||
Latest revision as of 16:57, 13 March 2024
Crystal structure of SoxR in complex with DNACrystal structure of SoxR in complex with DNA
Structural highlights
FunctionSOXR_ECOLI Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron-sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress. Upon reduction of 2Fe-2S cluster, SoxR reversibly loses its transcriptional activity, but retains its DNA binding affinity. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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