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6WIG

Structure of STENOFOLIA Protein HD domain bound with DNA

Summary for 6WIG
Entry DOI10.2210/pdb6wig/pdb
DescriptorSTENOFOLIA, DNA (5'-D(P*GP*CP*AP*AP*AP*TP*TP*AP*AP*TP*GP*AP*TP*TP*TP*AP*TP*TP*CP*AP*AP*G)-3'), DNA (5'-D(P*CP*TP*TP*GP*AP*AP*TP*AP*AP*AP*TP*CP*AP*TP*TP*AP*AP*TP*TP*TP*GP*C)-3'), ... (4 entities in total)
Functional Keywordsstf, hd domain, wox, transcriptional factor, plant protein, plant protein-dna complex, plant protein/dna
Biological sourceMedicago truncatula (Barrel medic)
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Total number of polymer chains4
Total formula weight38233.56
Authors
Deng, J.,Peng, S.,Pathak, P. (deposition date: 2020-04-09, release date: 2021-08-11, Last modification date: 2024-05-22)
Primary citationPathak, P.K.,Zhang, F.,Peng, S.,Niu, L.,Chaturvedi, J.,Elliott, J.,Xiang, Y.,Tadege, M.,Deng, J.
Structure of the unique tetrameric STENOFOLIA homeodomain bound with target promoter DNA.
Acta Crystallogr D Struct Biol, 77:1050-1063, 2021
Cited by
PubMed Abstract: Homeobox transcription factors are key regulators of morphogenesis and development in both animals and plants. In plants, the WUSCHEL-related homeobox (WOX) family of transcription factors function as central organizers of several developmental programs ranging from embryo patterning to meristematic stem-cell maintenance through transcriptional activation and repression mechanisms. The Medicago truncatula STENOFOLIA (STF) gene is a master regulator of leaf-blade lateral development. Here, the crystal structure of the homeodomain (HD) of STF (STF-HD) in complex with its promoter DNA is reported at 2.1 Å resolution. STF-HD binds DNA as a tetramer, enclosing nearly the entire bound DNA surface. The STF-HD tetramer is partially stabilized by docking of the C-terminal tail of one protomer onto a conserved hydrophobic surface on the head of another protomer in a head-to-tail manner. STF-HD specifically binds TGA motifs, although the promoter sequence also contains TAAT motifs. Helix α3 not only serves a canonical role as a base reader in the major groove, but also provides DNA binding in the minor groove through basic residues located at its C-terminus. The structural and functional data in planta reported here provide new insights into the DNA-binding mechanisms of plant-specific HDs from the WOX family of transcription factors.
PubMed: 34342278
DOI: 10.1107/S205979832100632X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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