3vod

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<StructureSection load='3vod' size='340' side='right'caption='[[3vod]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3vod' size='340' side='right'caption='[[3vod]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vod]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VOD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vod]] is a 2 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=3VOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VOD FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3voe|3voe]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1530, cfxB, inaR, JW5248, marR, soxQ ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vod OCA], [https://pdbe.org/3vod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vod RCSB], [https://www.ebi.ac.uk/pdbsum/3vod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vod ProSAT]</span></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=3vod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vod OCA], [https://pdbe.org/3vod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vod RCSB], [https://www.ebi.ac.uk/pdbsum/3vod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vod ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MARR_ECOLI MARR_ECOLI]] Repressor of the marRAB operon which is involved in the activation of both antibiotic resistance and oxidative stress genes. Binds to the marO operator/promoter site.
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[https://www.uniprot.org/uniprot/MARR_ECOLI MARR_ECOLI] Repressor of the marRAB operon which is involved in the activation of both antibiotic resistance and oxidative stress genes. Binds to the marO operator/promoter site.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The widely conserved multiple antibiotic resistance regulator (MarR) family of transcription factors modulates bacterial detoxification in response to diverse antibiotics, toxic chemicals or both. The natural inducer for Escherichia coli MarR, the prototypical transcription repressor within this family, remains unknown. Here we show that copper signaling potentiates MarR derepression in E. coli. Copper(II) oxidizes a cysteine residue (Cys80) on MarR to generate disulfide bonds between two MarR dimers, thereby inducing tetramer formation and the dissociation of MarR from its cognate promoter DNA. We further discovered that salicylate, a putative MarR inducer, and the clinically important bactericidal antibiotics norfloxacin and ampicillin all stimulate intracellular copper elevation, most likely through oxidative impairment of copper-dependent envelope proteins, including NADH dehydrogenase-2. This membrane-associated copper oxidation and liberation process derepresses MarR, causing increased bacterial antibiotic resistance. Our study reveals that this bacterial transcription regulator senses copper(II) as a natural signal to cope with stress caused by antibiotics or the environment.
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The multiple antibiotic resistance regulator MarR is a copper sensor in Escherichia coli.,Hao Z, Lou H, Zhu R, Zhu J, Zhang D, Zhao BS, Zeng S, Chen X, Chan J, He C, Chen PR Nat Chem Biol. 2014 Jan;10(1):21-8. doi: 10.1038/nchembio.1380. Epub 2013 Nov 3. PMID:24185215<ref>PMID:24185215</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3vod" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hao, Z]]
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[[Category: Hao Z]]
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[[Category: Lou, H]]
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[[Category: Lou H]]
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[[Category: Zhu, R]]
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[[Category: Zhu R]]
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[[Category: Transcription]]
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[[Category: Winged helix-turn-helix dna binding motif]]
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Current revision

Crystal Structure of mutant MarR C80S from E.coli

PDB ID 3vod

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