5hlg: Difference between revisions
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New page: '''Unreleased structure''' The entry 5hlg is ON HOLD Authors: Liu, G., Liu, X., Gan, J., Yang, C.G. Description: Structure of reduced AbfR bound to DNA [[Category: Unreleased Structure... |
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The | ==Structure of reduced AbfR bound to DNA== | ||
<StructureSection load='5hlg' size='340' side='right'caption='[[5hlg]], [[Resolution|resolution]] 3.00Å' 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]] 3Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5hlg" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Gan | <references/> | ||
[[Category: Liu | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus epidermidis]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Gan J]] | |||
[[Category: Liu G]] | |||
[[Category: Liu X]] | |||
[[Category: Yang CG]] | |||
Latest revision as of 10:45, 16 August 2023
Structure of reduced AbfR bound to DNA
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