8iex
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8iex]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IEX FirstGlance]. <br> | <table><tr><td colspan='2'>[[8iex]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IEX FirstGlance]. <br> | ||
- | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> |
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=8iex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8iex OCA], [https://pdbe.org/8iex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8iex RCSB], [https://www.ebi.ac.uk/pdbsum/8iex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8iex ProSAT]</span></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=8iex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8iex OCA], [https://pdbe.org/8iex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8iex RCSB], [https://www.ebi.ac.uk/pdbsum/8iex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8iex ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/WRK11_ARATH WRK11_ARATH] Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity). Regulates rhizobacterium B.cereus AR156-induced systemic resistance (ISR) to P.syringae pv. tomato DC3000, probably by activating the jasmonic acid (JA)- signaling pathway (PubMed:26433201).<ref>PMID:26433201</ref> | [https://www.uniprot.org/uniprot/WRK11_ARATH WRK11_ARATH] Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity). Regulates rhizobacterium B.cereus AR156-induced systemic resistance (ISR) to P.syringae pv. tomato DC3000, probably by activating the jasmonic acid (JA)- signaling pathway (PubMed:26433201).<ref>PMID:26433201</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The Arabidopsis WRKY11 (AtWRKY11) protein is an important transcription factor involved in plant response to biotic and abiotic stresses. Its DNA-binding domain specifically binds to gene promoter regions harboring the W-box consensus motif. Herein we report the high-resolution structure of the AtWRKY11 DNA-binding domain (DBD) determined by solution NMR spectroscopy. The results show that AtWRKY11-DBD adopts an all-beta fold comprising five beta-strands packed in an antiparallel topology, stabilized by a zinc-finger motif. Structural comparison reveals that the long beta(1)-beta(2) loop shows the highest structural variation from other available WRKY domain structures. Moreover, this loop was further found to contribute to the binding between AtWRKY11-DBD and W-box DNA. Our current study provides atomic-level structural basis for further understanding the structure-function relationship of plant WRKY proteins. | ||
+ | |||
+ | Solution structure of the DNA binding domain of Arabidopsis transcription factor WRKY11.,Wang J, Lin Y, Yang J, Zhang Q, Liu M, Hu Y, Dong X Biochem Biophys Res Commun. 2023 Apr 23;653:133-139. doi: , 10.1016/j.bbrc.2023.02.072. Epub 2023 Feb 26. PMID:36868077<ref>PMID:36868077</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 8iex" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> |
Current revision
Solution structure of AtWRKY11-DBD
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