7bzd: Difference between revisions
New page: '''Unreleased structure''' The entry 7bzd is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Structure of Bacillus subtilis HxlR, wild type== | |||
<StructureSection load='7bzd' size='340' side='right'caption='[[7bzd]], [[Resolution|resolution]] 2.61Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7bzd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BZD 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]] 2.612Å</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=7bzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bzd OCA], [https://pdbe.org/7bzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bzd RCSB], [https://www.ebi.ac.uk/pdbsum/7bzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bzd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HXLR_BACSU HXLR_BACSU] Positive regulator of hxlAB expression. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Formaldehyde (FA) has long been considered as a toxin and carcinogen due to its damaging effects to biological macromolecules, but its beneficial roles have been increasingly appreciated lately. Real-time monitoring of this reactive molecule in living systems is highly desired in order to decipher its physiological and/or pathological functions, but a genetically encoded FA sensor is currently lacking. We herein adopt a structure-based study of the underlying mechanism of the FA-responsive transcription factor HxlR from Bacillus subtilis, which shows that HxlR recognizes FA through an intra-helical cysteine-lysine crosslinking reaction at its N-terminal helix alpha1, leading to conformational change and transcriptional activation. By leveraging this FA-induced intra-helical crosslinking and gain-of-function reorganization, we develop the genetically encoded, reaction-based FA sensor-FAsor, allowing spatial-temporal visualization of FA in mammalian cells and mouse brain tissues. | |||
Genetically encoded formaldehyde sensors inspired by a protein intra-helical crosslinking reaction.,Zhu R, Zhang G, Jing M, Han Y, Li J, Zhao J, Li Y, Chen PR Nat Commun. 2021 Jan 25;12(1):581. doi: 10.1038/s41467-020-20754-4. PMID:33495458<ref>PMID:33495458</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7bzd" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]] | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis subsp. subtilis str. 168]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen PR]] | |||
[[Category: Zhu R]] | |||
Latest revision as of 18:44, 29 November 2023
Structure of Bacillus subtilis HxlR, wild typeStructure of Bacillus subtilis HxlR, wild type
Structural highlights
FunctionHXLR_BACSU Positive regulator of hxlAB expression. Publication Abstract from PubMedFormaldehyde (FA) has long been considered as a toxin and carcinogen due to its damaging effects to biological macromolecules, but its beneficial roles have been increasingly appreciated lately. Real-time monitoring of this reactive molecule in living systems is highly desired in order to decipher its physiological and/or pathological functions, but a genetically encoded FA sensor is currently lacking. We herein adopt a structure-based study of the underlying mechanism of the FA-responsive transcription factor HxlR from Bacillus subtilis, which shows that HxlR recognizes FA through an intra-helical cysteine-lysine crosslinking reaction at its N-terminal helix alpha1, leading to conformational change and transcriptional activation. By leveraging this FA-induced intra-helical crosslinking and gain-of-function reorganization, we develop the genetically encoded, reaction-based FA sensor-FAsor, allowing spatial-temporal visualization of FA in mammalian cells and mouse brain tissues. Genetically encoded formaldehyde sensors inspired by a protein intra-helical crosslinking reaction.,Zhu R, Zhang G, Jing M, Han Y, Li J, Zhao J, Li Y, Chen PR Nat Commun. 2021 Jan 25;12(1):581. doi: 10.1038/s41467-020-20754-4. PMID:33495458[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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