View source for 5hlg


==Structure of reduced AbfR bound to DNA==
<StructureSection load='5hlg' size='340' side='right'caption='[[5hlg]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5HKZ1_STAEQ Q5HKZ1_STAEQ] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:28086264</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hlg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus epidermidis]]
[[Category: Synthetic construct]]
[[Category: Gan J]]
[[Category: Liu G]]
[[Category: Liu X]]
[[Category: Yang CG]]