View source for 2jmw


==Structure of DNA-Binding Domain of Arabidopsis GT-1==
<StructureSection load='2jmw' size='340' side='right'caption='[[2jmw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jmw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JMW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2jmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jmw OCA], [https://pdbe.org/2jmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jmw RCSB], [https://www.ebi.ac.uk/pdbsum/2jmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jmw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TGT1_ARATH TGT1_ARATH] Probable transcription factor that binds specifically to the core DNA sequence 5'-GGTTAA-3'. May act as a molecular switch in response to light signals.<ref>PMID:10437822</ref> <ref>PMID:15044016</ref> <ref>PMID:7866025</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jm/2jmw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jmw ConSurf].
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
GT-1 is a plant transcription factor that binds to one of the cis-acting elements, BoxII, which resides within the upstream promoter region of light-responsive genes. GT-1 was assumed to act as a molecular switch modulated through Ca(2+)-dependent phosphorylation/dephosphorylation in response to light signals. It was shown previously that the phosphorylation of threonine 133 in the DNA-binding domain (DBD) of GT-1 results in enhancement of the BoxII-binding activity. Interestingly, point mutation of Thr133 to Asp also enhances the BoxII-binding activity. Here, we report the solution structures of hypothetical trihelix DBDs of the wild-type (WT) and a phosphomimetic mutant (T133D) of GT-1. First, we demonstrated that the isolated DBD of GT-1 alone has the ability to bind to DNA, and that the T133D mutation of the isolated DBD can enhance the DNA-binding affinity. The structures of these DBDs turned out to be almost identical. The structural topology resembles that of Myb DBDs, but all alpha-helices are longer in GT-1. Our NMR titration experiments suggested that these longer alpha-helices yield an enlarged DNA-binding surface. The phosphorylation site is located at the N-terminus of the third alpha-helix. We built a structural model of the T133D DBD:BoxII complex with the program HADDOCK. The model resembles the structure of the TRF1 DBD:telomeric DNA complex. Interestingly, the model implies that the phosphorylated side chain may directly interact with the bases of DNA. On the basis of our findings, we propose a mechanism by which the DNA-binding activity toward BoxII of the phosphorylated GT-1 could be enhanced.

Solution structures of the trihelix DNA-binding domains of the wild-type and a phosphomimetic mutant of Arabidopsis GT-1: mechanism for an increase in DNA-binding affinity through phosphorylation.,Nagata T, Niyada E, Fujimoto N, Nagasaki Y, Noto K, Miyanoiri Y, Murata J, Hiratsuka K, Katahira M Proteins. 2010 Nov 1;78(14):3033-47. PMID:20717979<ref>PMID:20717979</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2jmw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Hiratsuka K]]
[[Category: Ikeda Y]]
[[Category: Katahira M]]
[[Category: Murata J]]
[[Category: Nagata T]]
[[Category: Niyada E]]
[[Category: Noto K]]
[[Category: Uesugi S]]
[[Category: Yamamoto Y]]