View source for 8oj1


==Crystal structure of the DNA binding domain of M. polymorpha Auxin Response Factor 2 (MpARF2) in complex with High Affinity DNA==
<StructureSection load='8oj1' size='340' side='right'caption='[[8oj1]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8oj1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Marchantia_polymorpha Marchantia polymorpha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OJ1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.57&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=8oj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8oj1 OCA], [https://pdbe.org/8oj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8oj1 RCSB], [https://www.ebi.ac.uk/pdbsum/8oj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8oj1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0G3FH20_MARPO A0A0G3FH20_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]
<div style="background-color:#fffaf0;">
== 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<ref>PMID:40086441</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8oj1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Marchantia polymorpha]]
[[Category: Boer DR]]
[[Category: Crespo I]]
[[Category: Weijers D]]