6abt: Difference between revisions
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<StructureSection load='6abt' size='340' side='right'caption='[[6abt]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='6abt' size='340' side='right'caption='[[6abt]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6abt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ABT OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6abt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ABT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ABT FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=6abt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6abt OCA], [https://pdbe.org/6abt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6abt RCSB], [https://www.ebi.ac.uk/pdbsum/6abt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6abt ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/L8DXR9_LISMN L8DXR9_LISMN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6abt" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6abt" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Listeria monocytogenes]] | ||
[[Category: | [[Category: Hong M]] | ||
[[Category: | [[Category: Lee C]] | ||
Latest revision as of 12:24, 22 November 2023
Crystal structure of transcription factor from Listeria monocytogenesCrystal structure of transcription factor from Listeria monocytogenes
Structural highlights
FunctionPublication Abstract from PubMedListeria monocytogenes is a foodborne pathogen that causes listeriosis and can lead to serious clinical problems, such as sepsis and meningitis, in immunocompromised patients and neonates. Due to a growing number of antibiotic-resistant L. monocytogenes strains, listeriosis can steadily become refractory to antibiotic treatment. To develop novel therapeutics against listeriosis, the drug resistance mechanism of L. monocytogenes needs to be determined. The transcription factor LftR from L. monocytogenes regulates the expression of a putative multidrug resistance transporter, LieAB, and belongs to the PadR-2 subfamily of the PadR family. Despite the functional significance of LftR, our molecular understanding of the transcriptional regulatory mechanism for LftR and even for the PadR-2 subfamily is highly limited. Here, we report the crystal structure of LftR, which forms a dimer and protrudes two winged helix-turn-helix motifs for DNA recognition. Structure-based mutational and comparative analyses showed that LftR interacts with operator DNA through a LftR-specific mode as well as a common mechanism used by the PadR family. Moreover, the LftR dimer harbors one intersubunit cavity in the center of the dimeric structure as a putative ligand-binding site. Finally, conformational flexibilities in the LftR dimer and in the cavity suggest that a ligand-induced regulatory mechanism would be used by the LftR transcription factor. Structure-based molecular characterization and regulatory mechanism of the LftR transcription factor from Listeria monocytogenes: Conformational flexibilities and a ligand-induced regulatory mechanism.,Lee C, Kim MI, Park J, Hong M PLoS One. 2019 Apr 10;14(4):e0215017. doi: 10.1371/journal.pone.0215017., eCollection 2019. PMID:30970033[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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