8oj2 | pdb_00008oj2

Crystal structure of the DNA binding domain of M. polymorpha Auxin Response Factor 2 (MpARF2) in complex with protomor-like sequence IR7

spinqualitylabelsall models 8oj2, resolution 2.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8oj2 is a 2 chain structure with sequence from Marchantia polymorpha. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.56Å Ligands: CL, MES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A176WDW1_MARPO Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs).[RuleBase:RU004561] Publication Abstract from PubMed Plant development is primarily controlled by the auxin phytohormones, which activate the auxin response factors (ARFs). Although the nuclear auxin pathway (NAP) is well studied, little is known on how ARFs specifically select target genes. Here, we investigated the DNA binding mechanism of ARF DNA binding domains (DBDs) from the activator class A and repressor class B in two evolutionary distant plant species, Marchantia polymorpha and Arabidopsis thaliana using fluorescence anisotropy, size exclusion chromatography, macromolecular crystallography (MX), and small-angle X-ray scattering (SAXS). We find that the previously proposed molecular caliper model, which partially explains the variability in binding of the ARFs to DNA, has been preserved throughout evolution. Our results show that the DBD of class B MpARF2 behaves more like class A AtARF5 than class B AtARF1. These findings suggest that DNA recognition of ARFs has diverged independently of the transcriptional output, which has significant implications for understanding diverse responses to auxin. The structure and function of the DNA binding domain of class B MpARF2 share more traits with class A AtARF5 than to that of class B AtARF1.,Crespo I, Malfois M, Rienstra J, Tarres-Sole A, van den Berg W, Weijers D, Boer DR Structure. 2025 Mar 7:S0969-2126(25)00059-0. doi: 10.1016/j.str.2025.02.006. PMID:40086441 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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