7nmb: Difference between revisions
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==cytoplasmic domain of Vibrio cholerae ToxR== | ==cytoplasmic domain of Vibrio cholerae ToxR== | ||
<StructureSection load='7nmb' size='340' side='right'caption='[[7nmb]]' scene=''> | <StructureSection load='7nmb' size='340' side='right'caption='[[7nmb]], [[NMR_Ensembles_of_Models | 5 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full | <table><tr><td colspan='2'>[[7nmb]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NMB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NMB FirstGlance]. <br> | ||
</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=7nmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nmb OCA], [https://pdbe.org/7nmb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nmb RCSB], [https://www.ebi.ac.uk/pdbsum/7nmb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nmb ProSAT]</span></td></tr> | </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=7nmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nmb OCA], [https://pdbe.org/7nmb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nmb RCSB], [https://www.ebi.ac.uk/pdbsum/7nmb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nmb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ToxR represents an essential transcription factor of Vibrio cholerae, which is involved in the regulation of multiple, mainly virulence associated genes. Its versatile functionality as activator, respressor or co-activator suggests a complex regulatory mechanism, whose clarification is essential for a better understanding of the virulence expression system of V. cholerae. Here, we provide structural information elucidating the organization and binding behaviour of the cytoplasmic DNA binding domain of ToxR (cToxR), containing a winged helix-turn-helix (wHTH) motif. Our analysis reveals unexpected structural features of this domain expanding our knowledge of a poorly-defined subfamily of wHTH proteins. cToxR forms an extraordinary long alpha-loop and furthermore has an additional C-terminal beta strand, contacting the N-terminus and thus leading to a compact fold. The identification of the exact interactions between ToxR and DNA contributes to a deeper understanding of this regulatory process. Our findings not only show general binding of the soluble cytoplasmic domain of ToxR to DNA, but also indicate a higher affinity for the toxT motif. These results support the current theory of ToxR being a 'DNA-catcher' to enable binding of the transcription factor TcpP and thus activation of virulence-associated toxT transcription. Although, TcpP and ToxR interaction is assumed to be crucial in the activation of the toxT genes, we could not detect an interaction event of their isolated cytoplasmic domains. We therefore conclude that other factors are needed to establish this protein-protein interaction, e.g., membrane attachment, the presence of their full-length proteins and/or other intermediary proteins that may facilitate binding. | |||
Structural and DNA binding properties of the cytoplasmic domain of Vibrio cholerae transcription factor ToxR.,Gubensak N, Schrank E, Hartlmuller C, Gobl C, Falsone FS, Becker W, Wagner GE, Pulido S, Meyer NH, Pavkov-Keller T, Madl T, Reidl J, Zangger K J Biol Chem. 2021 Sep 3:101167. doi: 10.1016/j.jbc.2021.101167. PMID:34487759<ref>PMID:34487759</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7nmb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gubensaek N]] | [[Category: Gubensaek, N]] | ||
[[Category: Hartlmueller C]] | [[Category: Hartlmueller, C]] | ||
[[Category: Madl T]] | [[Category: Madl, T]] | ||
[[Category: Zangger K]] | [[Category: Zangger, K]] | ||
[[Category: Dna binding domain whth transcription factor]] | |||
[[Category: Transcription]] | |||
Revision as of 11:00, 10 November 2021
cytoplasmic domain of Vibrio cholerae ToxRcytoplasmic domain of Vibrio cholerae ToxR
Structural highlights
Publication Abstract from PubMedToxR represents an essential transcription factor of Vibrio cholerae, which is involved in the regulation of multiple, mainly virulence associated genes. Its versatile functionality as activator, respressor or co-activator suggests a complex regulatory mechanism, whose clarification is essential for a better understanding of the virulence expression system of V. cholerae. Here, we provide structural information elucidating the organization and binding behaviour of the cytoplasmic DNA binding domain of ToxR (cToxR), containing a winged helix-turn-helix (wHTH) motif. Our analysis reveals unexpected structural features of this domain expanding our knowledge of a poorly-defined subfamily of wHTH proteins. cToxR forms an extraordinary long alpha-loop and furthermore has an additional C-terminal beta strand, contacting the N-terminus and thus leading to a compact fold. The identification of the exact interactions between ToxR and DNA contributes to a deeper understanding of this regulatory process. Our findings not only show general binding of the soluble cytoplasmic domain of ToxR to DNA, but also indicate a higher affinity for the toxT motif. These results support the current theory of ToxR being a 'DNA-catcher' to enable binding of the transcription factor TcpP and thus activation of virulence-associated toxT transcription. Although, TcpP and ToxR interaction is assumed to be crucial in the activation of the toxT genes, we could not detect an interaction event of their isolated cytoplasmic domains. We therefore conclude that other factors are needed to establish this protein-protein interaction, e.g., membrane attachment, the presence of their full-length proteins and/or other intermediary proteins that may facilitate binding. Structural and DNA binding properties of the cytoplasmic domain of Vibrio cholerae transcription factor ToxR.,Gubensak N, Schrank E, Hartlmuller C, Gobl C, Falsone FS, Becker W, Wagner GE, Pulido S, Meyer NH, Pavkov-Keller T, Madl T, Reidl J, Zangger K J Biol Chem. 2021 Sep 3:101167. doi: 10.1016/j.jbc.2021.101167. PMID:34487759[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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