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7WQ5

Crystal structure of Arabidopsis transcriptional factor WRINKLED1 with dsDNA

Summary for 7WQ5
Entry DOI10.2210/pdb7wq5/pdb
DescriptorEthylene-responsive transcription factor WRI1, DNA (5'-D(P*GP*TP*GP*GP*AP*CP*GP*AP*TP*GP*AP*AP*AP*CP*CP*GP*AP*GP*GP*AP*AP*GP*TP*A)-3'), DNA (5'-D(P*TP*AP*CP*TP*TP*CP*CP*TP*CP*GP*GP*TP*TP*TP*CP*AP*TP*CP*GP*TP*CP*CP*AP*C)-3'), ... (5 entities in total)
Functional Keywordstranscriptional factor, dna binding protein
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains6
Total formula weight87901.39
Authors
Zhu, Q.,Gao, Y.G. (deposition date: 2022-01-24, release date: 2022-08-31, Last modification date: 2024-05-29)
Primary citationQiao, Z.,Kong, Q.,Tee, W.T.,Lim, A.R.Q.,Teo, M.X.,Olieric, V.,Low, P.M.,Yang, Y.,Qian, G.,Ma, W.,Gao, Y.G.
Molecular basis of the key regulator WRINKLED1 in plant oil biosynthesis.
Sci Adv, 8:eabq1211-eabq1211, 2022
Cited by
PubMed Abstract: Vegetable oils are not only major components of human diet but also vital for industrial applications. WRINKLED1 (WRI1) is a pivotal transcription factor governing plant oil biosynthesis, but the underlying DNA-binding mechanism remains incompletely understood. Here, we resolved the structure of Arabidopsis WRI1 (AtWRI1) with its cognate double-stranded DNA (dsDNA), revealing two antiparallel β sheets in the tandem AP2 domains that intercalate into the adjacent major grooves of dsDNA to determine the sequence recognition specificity. We showed that AtWRI1 represented a previously unidentified structural fold and DNA-binding mode. Mutations of the key residues interacting with DNA element affected its binding affinity and oil biosynthesis when these variants were transiently expressed in tobacco leaves. Seed oil content was enhanced in stable transgenic expressing an AtWRI1 variant (W74R). Together, our findings offer a structural basis explaining WRI1 recognition and binding of DNA and suggest an alternative strategy to increase oil yield in crops through WRI1 bioengineering.
PubMed: 36001661
DOI: 10.1126/sciadv.abq1211
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.35 Å)
Structure validation

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