3dte: Difference between revisions
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New page: '''Unreleased structure''' The entry 3dte is ON HOLD Authors: Vujicic-Zagar, A., Dulermo, R., Le Gorrec, M., Vannier, F., Servant, P., Sommer, S., de Groot, A., Serre, L. Description: ... |
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The | ==Crystal structure of the IRRE protein, a central regulator of DNA damage repair in deinococcaceae== | ||
<StructureSection load='3dte' size='340' side='right'caption='[[3dte]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3dte]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dsm_17065 Dsm 17065]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DTE FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dti|3dti]], [[3dtk|3dtk]]</div></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">irrE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=310783 DSM 17065])</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=3dte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dte OCA], [https://pdbe.org/3dte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dte RCSB], [https://www.ebi.ac.uk/pdbsum/3dte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dte ProSAT]</span></td></tr> | |||
</table> | |||
== 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/dt/3dte_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=3dte ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Deinococcaceae are famous for their extreme radioresistance. Transcriptome analysis in Deinococcus radiodurans revealed a group of genes up-regulated in response to desiccation and ionizing radiation. IrrE, a novel protein initially found in D. radiodurans, was shown to be a positive regulator of some of these genes. Deinococcus deserti irrE is able to restore radioresistance in a D. radiodurans DeltairrE mutant. The D. deserti IrrE crystal structure reveals a unique combination of three domains: one zinc peptidase-like domain, one helix-turn-helix motif and one GAF-like domain. Mutant analysis indicates that the first and third domains are critical regions for radiotolerance. In particular, mutants affected in the putative zinc-binding site are as sensitive to gamma and UV irradiation as the DeltairrE bacteria, and radioresistance is strongly decreased with the H217L mutation present in the C-terminal domain. In addition, modeling of IrrE-DNA interaction suggests that the observed IrrE structure may not bind double-stranded DNA through its central helix-turn-helix motif and that IrrE is not a classic transcriptional factor that activates gene expression by its direct binding to DNA. We propose that the putative protease activity of IrrE could be a key element of transcription enhancement and that a more classic transcription factor, possibly an IrrE substrate, would link IrrE to transcription of genes specifically involved in radioresistance. | |||
Crystal Structure of the IrrE Protein, a Central Regulator of DNA Damage Repair in Deinococcaceae.,Vujicic-Zagar A, Dulermo R, Le Gorrec M, Vannier F, Servant P, Sommer S, de Groot A, Serre L J Mol Biol. 2009 Jan 3. PMID:19150362<ref>PMID:19150362</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3dte" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dsm 17065]] | |||
[[Category: Large Structures]] | |||
[[Category: Dulermo, R]] | |||
[[Category: Gorrec, M Le]] | |||
[[Category: Groot, A De]] | |||
[[Category: Serre, L]] | |||
[[Category: Servant, P]] | |||
[[Category: Sommer, S]] | |||
[[Category: Vannier, F]] | |||
[[Category: Vujicic-Zagar, A]] | |||
[[Category: Deinococcus]] | |||
[[Category: Gene regulation]] | |||
[[Category: Irre]] | |||
[[Category: Metallopeptidase]] | |||
[[Category: Radiotolerance]] | |||
