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| | ==Crystal structure of E.coli NemR reduced form== | | ==Crystal structure of E.coli NemR reduced form== |
| - | <StructureSection load='4yze' size='340' side='right' caption='[[4yze]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4yze' size='340' side='right'caption='[[4yze]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4yze]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YZE FirstGlance]. <br> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nemR, ydhM, b1649, JW5874 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | </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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yze OCA], [http://pdbe.org/4yze PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yze RCSB], [http://www.ebi.ac.uk/pdbsum/4yze PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yze ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4yze" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4yze" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Gray, M J]] | + | [[Category: Large Structures]] |
| - | [[Category: Jakob, U]] | + | [[Category: Gray MJ]] |
| - | [[Category: Li, Y]] | + | [[Category: Jakob U]] |
| - | [[Category: Xu, Z]] | + | [[Category: Li Y]] |
| - | [[Category: Cystein-lysine sulfenamide thiol]]
| + | [[Category: Xu Z]] |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription factor]]
| + | |
| Structural highlights
Function
NEMR_ECOLI Represses the transcription of the nemRA operon by binding to the nemR box.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Umezawa Y, Shimada T, Kori A, Yamada K, Ishihama A. The uncharacterized transcription factor YdhM is the regulator of the nemA gene, encoding N-ethylmaleimide reductase. J Bacteriol. 2008 Sep;190(17):5890-7. doi: 10.1128/JB.00459-08. Epub 2008 Jun 20. PMID:18567656 doi:http://dx.doi.org/10.1128/JB.00459-08
- ↑ Gray MJ, Li Y, Leichert LI, Xu Z, Jakob U. Does the Transcription Factor NemR Use a Regulatory Sulfenamide Bond to Sense Bleach? Antioxid Redox Signal. 2015 Sep 20;23(9):747-54. doi: 10.1089/ars.2015.6346. Epub, 2015 Jun 22. PMID:25867078 doi:http://dx.doi.org/10.1089/ars.2015.6346
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