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| <StructureSection load='1ut7' size='340' side='right'caption='[[1ut7]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1ut7' size='340' side='right'caption='[[1ut7]], [[Resolution|resolution]] 1.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1ut7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UT7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UT7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ut7]] is a 2 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=1UT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UT7 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene></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]] 1.9Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ut4|1ut4]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ut7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ut7 OCA], [http://pdbe.org/1ut7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ut7 RCSB], [http://www.ebi.ac.uk/pdbsum/1ut7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ut7 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=1ut7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ut7 OCA], [https://pdbe.org/1ut7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ut7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ut7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ut7 ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/NAC19_ARATH NAC19_ARATH] Transcription factors that bind specifically to the 5'-CATGTG-3' motif.<ref>PMID:15319476</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: Large Structures]] | |
- | [[Category: Ernst, H A]] | |
- | [[Category: Larsen, S]] | |
- | [[Category: Leggio, L Lo]] | |
- | [[Category: Olsen, A N]] | |
- | [[Category: Skriver, K]] | |
- | [[Category: Abscisic acid response]] | |
| [[Category: Arabidopsis thaliana]] | | [[Category: Arabidopsis thaliana]] |
- | [[Category: Dna binding]] | + | [[Category: Large Structures]] |
- | [[Category: Nac domain]] | + | [[Category: Ernst HA]] |
- | [[Category: Transcription]] | + | [[Category: Larsen S]] |
- | [[Category: Transcription factor]] | + | [[Category: Lo Leggio L]] |
- | [[Category: Transcription regulation]] | + | [[Category: Olsen AN]] |
| + | [[Category: Skriver K]] |
| Structural highlights
Function
NAC19_ARATH Transcription factors that bind specifically to the 5'-CATGTG-3' motif.[1]
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
The structure of the DNA-binding NAC domain of Arabidopsis ANAC (abscisic-acid-responsive NAC) has been determined by X-ray crystallography to 1.9A resolution (Protein Data Bank codes 1UT4 and 1UT7). This is the first structure determined for a member of the NAC family of plant-specific transcriptional regulators. NAC proteins are characterized by their conserved N-terminal NAC domains that can bind both DNA and other proteins. NAC proteins are involved in developmental processes, including formation of the shoot apical meristem, floral organs and lateral shoots, as well as in plant hormonal control and defence. The NAC domain does not possess a classical helix-turn-helix motif; instead it reveals a new transcription factor fold consisting of a twisted beta-sheet surrounded by a few helical elements. The functional dimer formed by the NAC domain was identified in the structure, which will serve as a structural template for understanding NAC protein function at the molecular level.
Structure of the conserved domain of ANAC, a member of the NAC family of transcription factors.,Ernst HA, Olsen AN, Larsen S, Lo Leggio L EMBO Rep. 2004 Mar;5(3):297-303. PMID:15083810[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tran LS, Nakashima K, Sakuma Y, Simpson SD, Fujita Y, Maruyama K, Fujita M, Seki M, Shinozaki K, Yamaguchi-Shinozaki K. Isolation and functional analysis of Arabidopsis stress-inducible NAC transcription factors that bind to a drought-responsive cis-element in the early responsive to dehydration stress 1 promoter. Plant Cell. 2004 Sep;16(9):2481-98. Epub 2004 Aug 19. PMID:15319476 doi:http://dx.doi.org/10.1105/tpc.104.022699
- ↑ Ernst HA, Olsen AN, Larsen S, Lo Leggio L. Structure of the conserved domain of ANAC, a member of the NAC family of transcription factors. EMBO Rep. 2004 Mar;5(3):297-303. PMID:15083810 doi:10.1038/sj.embor.7400093
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