4nj6: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4nj6]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NJ6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4nj6]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NJ6 FirstGlance]. <br>
</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=4nj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nj6 OCA], [https://pdbe.org/4nj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nj6 RCSB], [https://www.ebi.ac.uk/pdbsum/4nj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nj6 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=4nj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nj6 OCA], [https://pdbe.org/4nj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nj6 RCSB], [https://www.ebi.ac.uk/pdbsum/4nj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nj6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/ARFG_ARATH ARFG_ARATH] Auxin response factors (ARFs) are transcriptional factors that binds specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Seems to act as transcriptional activator. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression. Required for differential growth responses of aerial tissues. Involved in ethylene responses. Regulates lateral root formation through direct regulation of LBD16 and/or LBD29. Functionally redundant with ARF19. Mediates embryo axis formation and vascular tissues differentiation. Functionally redundant with ARF7.<ref>PMID:12036261</ref> <ref>PMID:14973283</ref> <ref>PMID:16461383</ref> <ref>PMID:17259263</ref>  
[https://www.uniprot.org/uniprot/ARFG_ARATH ARFG_ARATH] Auxin response factors (ARFs) are transcriptional factors that binds specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Seems to act as transcriptional activator. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression. Required for differential growth responses of aerial tissues. Involved in ethylene responses. Regulates lateral root formation through direct regulation of LBD16 and/or LBD29. Functionally redundant with ARF19. Mediates embryo axis formation and vascular tissues differentiation. Functionally redundant with ARF7.<ref>PMID:12036261</ref> <ref>PMID:14973283</ref> <ref>PMID:16461383</ref> <ref>PMID:17259263</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In plants, the AUXIN RESPONSE FACTOR (ARF) transcription factor family regulates gene expression in response to auxin. In the absence of auxin, ARF transcription factors are repressed by interaction with AUXIN/INDOLE 3-ACETIC ACID (Aux/IAA) proteins. Although the C termini of ARF and Aux/IAA proteins facilitate their homo- and heterooligomerization, the molecular basis for this interaction remained undefined. The crystal structure of the C-terminal interaction domain of Arabidopsis ARF7 reveals a Phox and Bem1p (PB1) domain that provides both positive and negative electrostatic interfaces for directional protein interaction. Mutation of interface residues in the ARF7 PB1 domain yields monomeric protein and abolishes interaction with both itself and IAA17. Expression of a stabilized Aux/IAA protein (i.e., IAA16) bearing PB1 mutations in Arabidopsis suggests a multimerization requirement for ARF protein repression, leading to a refined auxin-signaling model.
Molecular basis for AUXIN RESPONSE FACTOR protein interaction and the control of auxin response repression.,Korasick DA, Westfall CS, Lee SG, Nanao MH, Dumas R, Hagen G, Guilfoyle TJ, Jez JM, Strader LC Proc Natl Acad Sci U S A. 2014 Apr 8;111(14):5427-32. doi:, 10.1073/pnas.1400074111. Epub 2014 Mar 25. PMID:24706860<ref>PMID:24706860</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4nj6" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 12:33, 1 March 2024

PB1 Domain of AtARF7

4nj6, resolution 2.40Å

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