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[[Image:2q1z.gif|left|200px]]


{{Structure
==Crystal Structure of Rhodobacter sphaeroides SigE in complex with the anti-sigma ChrR==
|PDB= 2q1z |SIZE=350|CAPTION= <scene name='initialview01'>2q1z</scene>, resolution 2.40&Aring;
<StructureSection load='2q1z' size='340' side='right'caption='[[2q1z]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
<table><tr><td colspan='2'>[[2q1z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides_2.4.1 Cereibacter sphaeroides 2.4.1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q1Z FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
|GENE= rpoE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]), chrR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2q1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q1z OCA], [https://pdbe.org/2q1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q1z RCSB], [https://www.ebi.ac.uk/pdbsum/2q1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q1z ProSAT]</span></td></tr>
|RELATEDENTRY=[[2z2s|2Z2S]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q1z OCA], [http://www.ebi.ac.uk/pdbsum/2q1z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q1z RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/RPOE_CERS4 RPOE_CERS4] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor until released. Sigma-E controls a transcriptional response to singlet oxygen, a by-product of photosynthesis; its continuous activity requires constant exposure to singlet oxygen. The regulon has about 180 genes that protect against or repair damage induced by singlet oxygen, including itself and rpoH2, a heat shock-responsive sigma factor.<ref>PMID:11676534</ref> <ref>PMID:15855269</ref> <ref>PMID:17803943</ref>
 
== Evolutionary Conservation ==
'''Crystal Structure of Rhodobacter sphaeroides SigE in complex with the anti-sigma ChrR'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q1/2q1z_consurf.spt"</scriptWhenChecked>
A transcriptional response to singlet oxygen in Rhodobacter sphaeroides is controlled by the group IV sigma factor sigma(E) and its cognate anti-sigma ChrR. Crystal structures of the sigma(E)/ChrR complex reveal a modular, two-domain architecture for ChrR. The ChrR N-terminal anti-sigma domain (ASD) binds a Zn(2+) ion, contacts sigma(E), and is sufficient to inhibit sigma(E)-dependent transcription. The ChrR C-terminal domain adopts a cupin fold, can coordinate an additional Zn(2+), and is required for the transcriptional response to singlet oxygen. Structure-based sequence analyses predict that the ASD defines a common structural fold among predicted group IV anti-sigmas. These ASDs are fused to diverse C-terminal domains that are likely involved in responding to specific environmental signals that control the activity of their cognate sigma factor.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
2Q1Z is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q1Z OCA].  
</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=2q1z ConSurf].
 
<div style="clear:both"></div>
==Reference==
== References ==
A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria., Campbell EA, Greenwell R, Anthony JR, Wang S, Lim L, Das K, Sofia HJ, Donohue TJ, Darst SA, Mol Cell. 2007 Sep 7;27(5):793-805. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17803943 17803943]
<references/>
[[Category: Protein complex]]
__TOC__
[[Category: Rhodobacter sphaeroides]]
</StructureSection>
[[Category: Campbell, E A.]]
[[Category: Cereibacter sphaeroides 2 4.1]]
[[Category: Darst, S A.]]
[[Category: Large Structures]]
[[Category: anti-sigma factor]]
[[Category: Campbell EA]]
[[Category: cupin fold]]
[[Category: Darst SA]]
[[Category: ecf sigma factor]]
[[Category: zinc binding transcription factor]]
 
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