4dul: Difference between revisions
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==ANAC019 NAC domain crystal form IV== | ==ANAC019 NAC domain crystal form IV== | ||
<StructureSection load='4dul' size='340' side='right' caption='[[4dul]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4dul' size='340' side='right'caption='[[4dul]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4dul]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4dul]] 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=4DUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DUL FirstGlance]. <br> | ||
</td></tr> | </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=4dul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dul OCA], [https://pdbe.org/4dul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dul RCSB], [https://www.ebi.ac.uk/pdbsum/4dul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dul ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4dul" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4dul" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[NAC transcription factor|NAC transcription factor]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arabidopsis thaliana]] | ||
[[Category: Helgstrand | [[Category: Large Structures]] | ||
[[Category: Leggio | [[Category: Helgstrand C]] | ||
[[Category: Olsen | [[Category: Lo Leggio L]] | ||
[[Category: Skriver | [[Category: Olsen AN]] | ||
[[Category: Welner | [[Category: Skriver K]] | ||
[[Category: Welner D]] | |||
Revision as of 11:39, 21 September 2022
ANAC019 NAC domain crystal form IVANAC019 NAC domain crystal form IV
Structural highlights
Function[NAC19_ARATH] Transcription factors that bind specifically to the 5'-CATGTG-3' motif.[1] Publication Abstract from PubMedNAC (NAM/ATAF/CUC) plant transcription factors regulate essential processes in development, stress responses and nutrient distribution in important crop and model plants (rice, Populus, Arabidopsis), which makes them highly relevant in the context of crop optimization and bioenergy production. The structure of the DNA-binding NAC domain of ANAC019 has previously been determined by X-ray crystallography, revealing a dimeric and predominantly beta-fold structure, but the mode of binding to cognate DNA has remained elusive. In this study, information from low resolution X-ray structures and small angle X-ray scattering on complexes with oligonucleotides, mutagenesis and (DNaseI and uranyl photo-) footprinting, is combined to form a structural view of DNA-binding, and for the first time provide experimental evidence for the speculated relationship between plant specific NAC proteins, WRKY transcription factors and the mammalian GCM transcription factors, which all use a b-strand motif for DNA-binding. The structure shows how the NAC domain inserts the edge of its core beta-sheet in the major groove, while leaving the DNA largely un-distorted. The structure of the NAC-DNA complex and a new crystal form of the unbound NAC also indicate limited flexibility of the NAC dimer arrangement which could be important in recognizing suboptimal binding sites. DNA binding by the plant specific NAC transcription factors in crystal and solution: a firm link to WRKY and GCM transcription factors.,Welner DH, Lindemose S, Grossmann JG, Mollegaard NE, Olsen AN, Helgstrand C, Skriver K, Lo Leggio L Biochem J. 2012 Mar 29. PMID:22455904[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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