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4yze
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of E.coli NemR reduced form== | |
| + | <StructureSection load='4yze' size='340' side='right'caption='[[4yze]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4yze]] is a 4 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=4YZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YZE 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]] 2.2Å</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=4yze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yze OCA], [https://pdbe.org/4yze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yze RCSB], [https://www.ebi.ac.uk/pdbsum/4yze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yze ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NEMR_ECOLI NEMR_ECOLI] Represses the transcription of the nemRA operon by binding to the nemR box.<ref>PMID:18567656</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Reactive chlorine species (RCS), such as hypochlorous acid (i.e., bleach), are antimicrobial oxidants produced by the innate immune system. Like many redox-regulated transcription factors, the Escherichia coli repressor NemR responds to RCS by using the reversible oxidation of highly conserved cysteines to alter its DNA-binding affinity. However, earlier work showed that RCS response in NemR does not depend on any commonly known oxidative cysteine modifications. We have now determined the crystal structure of NemR, showing that the regulatory cysteine, Cys106, is in close proximity to a highly conserved lysine (Lys175). We used crystallographic, biochemical, and mass spectrometric analyses to analyze the role of this lysine residue in RCS sensing. Based on our results, we hypothesize that RCS treatment of NemR results in the formation of a reversible Cys106-Lys175 sulfenamide bond. This is, to our knowledge, the first description of a protein whose function is regulated by a cysteine-lysine sulfenamide thiol switch, constituting a novel addition to the biological repertoire of functional redox switches. | ||
| - | + | Does the Transcription Factor NemR Use a Regulatory Sulfenamide Bond to Sense Bleach?,Gray MJ, Li Y, Leichert LI, Xu Z, Jakob U Antioxid Redox Signal. 2015 Sep 20;23(9):747-54. doi: 10.1089/ars.2015.6346. Epub, 2015 Jun 22. PMID:25867078<ref>PMID:25867078</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4yze" style="background-color:#fffaf0;"></div> |
| - | [[Category: Jakob | + | |
| - | [[Category: | + | ==See Also== |
| - | [[Category: | + | *[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]] |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gray MJ]] | ||
| + | [[Category: Jakob U]] | ||
| + | [[Category: Li Y]] | ||
| + | [[Category: Xu Z]] | ||
Current revision
Crystal structure of E.coli NemR reduced form
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