5d8c: Difference between revisions
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==Crystal structure of HiNmlR, a MerR family regulator lacking the sensor domain, bound to promoter DNA== | |||
<StructureSection load='5d8c' size='340' side='right'caption='[[5d8c]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5d8c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D8C 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]] 2.25Å</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=5d8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d8c OCA], [https://pdbe.org/5d8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d8c RCSB], [https://www.ebi.ac.uk/pdbsum/5d8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d8c ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Y186_HAEIN Y186_HAEIN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pathogenic bacteria such as Haemophilus influenzae, a major cause of lower respiratory tract diseases, must cope with a range of electrophiles generated in the host or by endogenous metabolism. Formaldehyde is one such compound that can irreversibly damage proteins and DNA through alkylation and cross-linking and interfere with redox homeostasis. Its detoxification operates under the control of HiNmlR, a protein from the MerR family that lacks a specific sensor region and does not bind metal ions. We demonstrate that HiNmlR is a thiol-dependent transcription factor that modulates H. influenzae response to formaldehyde, with two cysteine residues (Cys54 and Cys71) identified to be important for its response against a formaldehyde challenge. We obtained crystal structures of HiNmlR in both the DNA-free and two DNA-bound forms, which suggest that HiNmlR enhances target gene transcription by twisting of operator DNA sequences in a two-gene operon containing overlapping promoters. Our work provides the first structural insights into the mechanism of action of MerR regulators that lack sensor regions. | |||
Structural basis of thiol-based regulation of formaldehyde detoxification in H. influenzae by a MerR regulator with no sensor region.,Counago RM, Chen NH, Chang CW, Djoko KY, McEwan AG, Kobe B Nucleic Acids Res. 2016 Jun 15. pii: gkw543. PMID:27307602<ref>PMID:27307602</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5d8c" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Haemophilus influenzae Rd KW20]] | |||
[[Category: Large Structures]] | |||
[[Category: Chang CW]] | |||
[[Category: Chen NH]] | |||
[[Category: Counago RM]] | |||
[[Category: Djoko KY]] | |||
[[Category: Kobe B]] | |||
[[Category: McEwan AG]] | |||
Latest revision as of 11:44, 27 September 2023
Crystal structure of HiNmlR, a MerR family regulator lacking the sensor domain, bound to promoter DNACrystal structure of HiNmlR, a MerR family regulator lacking the sensor domain, bound to promoter DNA
Structural highlights
FunctionPublication Abstract from PubMedPathogenic bacteria such as Haemophilus influenzae, a major cause of lower respiratory tract diseases, must cope with a range of electrophiles generated in the host or by endogenous metabolism. Formaldehyde is one such compound that can irreversibly damage proteins and DNA through alkylation and cross-linking and interfere with redox homeostasis. Its detoxification operates under the control of HiNmlR, a protein from the MerR family that lacks a specific sensor region and does not bind metal ions. We demonstrate that HiNmlR is a thiol-dependent transcription factor that modulates H. influenzae response to formaldehyde, with two cysteine residues (Cys54 and Cys71) identified to be important for its response against a formaldehyde challenge. We obtained crystal structures of HiNmlR in both the DNA-free and two DNA-bound forms, which suggest that HiNmlR enhances target gene transcription by twisting of operator DNA sequences in a two-gene operon containing overlapping promoters. Our work provides the first structural insights into the mechanism of action of MerR regulators that lack sensor regions. Structural basis of thiol-based regulation of formaldehyde detoxification in H. influenzae by a MerR regulator with no sensor region.,Counago RM, Chen NH, Chang CW, Djoko KY, McEwan AG, Kobe B Nucleic Acids Res. 2016 Jun 15. pii: gkw543. PMID:27307602[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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