8iex
From Proteopedia
Solution structure of AtWRKY11-DBD
Structural highlights
FunctionWRK11_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).[1] Publication Abstract from PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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