4fxe
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4fxe is ON HOLD Authors: Brodersen, D.E., Boggild, A., Sofos, N. Description: Crystal structure of the intact E. coli RelBE toxin-antitoxin complex) |
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of the intact E. coli RelBE toxin-antitoxin complex== | |
- | + | <StructureSection load='4fxe' size='340' side='right'caption='[[4fxe]], [[Resolution|resolution]] 2.75Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[4fxe]] is a 6 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=4FXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FXE 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]] 2.7503Å</td></tr> | |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4fxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxe OCA], [https://pdbe.org/4fxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fxe RCSB], [https://www.ebi.ac.uk/pdbsum/4fxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fxe ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/RELB_ECOLI RELB_ECOLI] Antitoxin component of a toxin-antitoxin (TA) module. Counteracts the effect of RelE via direct protein-protein interaction, enabling the reversion of translation inhibition. Also acts as an autorepressor of relBE transcription. DNA-binding and repression is stronger when complexed with corepressor RelE. Increased transcription rate of relBE and activation of relE is consistent with a lower level of RelB in starved cells due to degradation of RelB by protease Lon.<ref>PMID:9767574</ref> <ref>PMID:11274135</ref> <ref>PMID:11717402</ref> <ref>PMID:12123459</ref> <ref>PMID:19707553</ref> Seems to be a principal mediator of cell death in liquid media.<ref>PMID:9767574</ref> <ref>PMID:11274135</ref> <ref>PMID:11717402</ref> <ref>PMID:12123459</ref> <ref>PMID:19707553</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Escherichia coli K-12]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Boggild A]] | ||
+ | [[Category: Brodersen DE]] | ||
+ | [[Category: Sofos N]] |
Current revision
Crystal structure of the intact E. coli RelBE toxin-antitoxin complex
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