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| | <StructureSection load='5hlg' size='340' side='right'caption='[[5hlg]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='5hlg' size='340' side='right'caption='[[5hlg]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hlg]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/"albococcus_epidermidis"_winslow_and_winslow_1908 "albococcus epidermidis" winslow and winslow 1908]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HLG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HLG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hlg]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_epidermidis Staphylococcus epidermidis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HLG FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hlh|5hlh]], [[5hli|5hli]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADT70_02765, SETS_06435 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1282 "Albococcus epidermidis" Winslow and Winslow 1908])</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=5hlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hlg OCA], [https://pdbe.org/5hlg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hlg RCSB], [https://www.ebi.ac.uk/pdbsum/5hlg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hlg ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hlg OCA], [http://pdbe.org/5hlg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hlg RCSB], [http://www.ebi.ac.uk/pdbsum/5hlg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hlg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5HKZ1_STAEQ Q5HKZ1_STAEQ] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Albococcus epidermidis winslow and winslow 1908]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gan, J]] | + | [[Category: Staphylococcus epidermidis]] |
| - | [[Category: Liu, G]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Liu, X]] | + | [[Category: Gan J]] |
| - | [[Category: Yang, C G]] | + | [[Category: Liu G]] |
| - | [[Category: Transcription regulator-dna complex]] | + | [[Category: Liu X]] |
| | + | [[Category: Yang CG]] |
| Structural highlights
Function
Q5HKZ1_STAEQ
Publication Abstract from PubMed
As a master redox-sensing MarR-family transcriptional regulator, AbfR participates in oxidative stress responses and virulence regulations in Staphylococcus epidermidis. Here, we present structural insights into the DNA-binding mechanism of AbfR in different oxidation states by determining the X-ray crystal structures of a reduced-AbfR/DNA complex, an overoxidized (Cys13-SO2H and Cys13-SO3H) AbfR/DNA, and 2-disulfide cross-linked AbfR dimer. Together with biochemical analyses, our results suggest that the redox regulation of AbfR-sensing displays two novel features: (i) the reversible disulfide modification, but not the irreversible overoxidation, significantly abolishes the DNA-binding ability of the AbfR repressor; (ii) either 1-disulfide cross-linked or 2-disulfide cross-linked AbfR dimer is biologically significant. The overoxidized species of AbfR, resembling the reduced AbfR in conformation and retaining the DNA-binding ability, does not exist in biologically significant concentrations, however. The 1-disulfide cross-linked modification endows AbfR with significantly weakened capability for DNA-binding. The 2-disulfide cross-linked AbfR adopts a very "open" conformation that is incompatible with DNA-binding. Overall, the concise oxidation chemistry of the redox-active cysteine allows AbfR to sense and respond to oxidative stress correctly and efficiently.
Structural Insights into the Redox-Sensing Mechanism of MarR-Type Regulator AbfR.,Liu G, Liu X, Xu H, Liu X, Zhou H, Huang Z, Gan J, Chen H, Lan L, Yang CG J Am Chem Soc. 2017 Jan 23. doi: 10.1021/jacs.6b11438. PMID:28086264[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu G, Liu X, Xu H, Liu X, Zhou H, Huang Z, Gan J, Chen H, Lan L, Yang CG. Structural Insights into the Redox-Sensing Mechanism of MarR-Type Regulator AbfR. J Am Chem Soc. 2017 Jan 23. doi: 10.1021/jacs.6b11438. PMID:28086264 doi:http://dx.doi.org/10.1021/jacs.6b11438
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