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| | ==Structure of DNA-Binding Domain of Arabidopsis GT-1== | | ==Structure of DNA-Binding Domain of Arabidopsis GT-1== |
| - | <StructureSection load='2jmw' size='340' side='right'caption='[[2jmw]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2jmw' size='340' side='right'caption='[[2jmw]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jmw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. 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> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">T6J4.18 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | </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> | | <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> | | </table> |
| | == Function == | | == 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>
| + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hiratsuka, K]] | + | [[Category: Hiratsuka K]] |
| - | [[Category: Ikeda, Y]] | + | [[Category: Ikeda Y]] |
| - | [[Category: Katahira, M]] | + | [[Category: Katahira M]] |
| - | [[Category: Murata, J]] | + | [[Category: Murata J]] |
| - | [[Category: Nagata, T]] | + | [[Category: Nagata T]] |
| - | [[Category: Niyada, E]] | + | [[Category: Niyada E]] |
| - | [[Category: Noto, K]] | + | [[Category: Noto K]] |
| - | [[Category: Uesugi, S]] | + | [[Category: Uesugi S]] |
| - | [[Category: Yamamoto, Y]] | + | [[Category: Yamamoto Y]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna-binding domain]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| Structural highlights
Function
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.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Marechal E, Hiratsuka K, Delgado J, Nairn A, Qin J, Chait BT, Chua NH. Modulation of GT-1 DNA-binding activity by calcium-dependent phosphorylation. Plant Mol Biol. 1999 Jun;40(3):373-86. PMID:10437822
- ↑ Ayadi M, Delaporte V, Li YF, Zhou DX. Analysis of GT-3a identifies a distinct subgroup of trihelix DNA-binding transcription factors in Arabidopsis. FEBS Lett. 2004 Mar 26;562(1-3):147-54. PMID:15044016 doi:http://dx.doi.org/10.1016/S0014-5793(04)00222-4
- ↑ Hiratsuka K, Wu X, Fukuzawa H, Chua NH. Molecular dissection of GT-1 from Arabidopsis. Plant Cell. 1994 Dec;6(12):1805-13. PMID:7866025 doi:http://dx.doi.org/10.1105/tpc.6.12.1805
- ↑ Nagata T, Niyada E, Fujimoto N, Nagasaki Y, Noto K, Miyanoiri Y, Murata J, Hiratsuka K, Katahira M. 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. Proteins. 2010 Nov 1;78(14):3033-47. PMID:20717979 doi:10.1002/prot.22827
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