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| | <StructureSection load='4onq' size='340' side='right'caption='[[4onq]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='4onq' size='340' side='right'caption='[[4onq]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4onq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/American_tobacco American tobacco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ONQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ONQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4onq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ONQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ONQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</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]] 2.502Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4onj|4onj]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DRM, NtDRM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4097 American tobacco])</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=4onq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4onq OCA], [https://pdbe.org/4onq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4onq RCSB], [https://www.ebi.ac.uk/pdbsum/4onq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4onq ProSAT]</span></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=4onq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4onq OCA], [http://pdbe.org/4onq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4onq RCSB], [http://www.ebi.ac.uk/pdbsum/4onq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4onq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q76KU6_TOBAC Q76KU6_TOBAC] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[DNA methyltransferase|DNA methyltransferase]] | + | *[[DNA methyltransferase 3D structures|DNA methyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: American tobacco]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Du, J]] | + | [[Category: Nicotiana tabacum]] |
| - | [[Category: Patel, D J]] | + | [[Category: Du J]] |
| - | [[Category: Dna methyltransferase]] | + | [[Category: Patel DJ]] |
| - | [[Category: Transferase-transferase inhibitor complex]]
| + | |
| Structural highlights
Function
Q76KU6_TOBAC
Publication Abstract from PubMed
DNA methylation is a conserved epigenetic gene-regulation mechanism. DOMAINS REARRANGED METHYLTRANSFERASE (DRM) is a key de novo methyltransferase in plants, but how DRM acts mechanistically is poorly understood. Here, we report the crystal structure of the methyltransferase domain of tobacco DRM (NtDRM) and reveal a molecular basis for its rearranged structure. NtDRM forms a functional homodimer critical for catalytic activity. We also show that Arabidopsis DRM2 exists in complex with the small interfering RNA (siRNA) effector ARGONAUTE4 (AGO4) and preferentially methylates one DNA strand, likely the strand acting as the template for RNA polymerase V-mediated noncoding RNA transcripts. This strand-biased DNA methylation is also positively correlated with strand-biased siRNA accumulation. These data suggest a model in which DRM2 is guided to target loci by AGO4-siRNA and involves base-pairing of associated siRNAs with nascent RNA transcripts.
Molecular Mechanism of Action of Plant DRM De Novo DNA Methyltransferases.,Zhong X, Du J, Hale CJ, Gallego-Bartolome J, Feng S, Vashisht AA, Chory J, Wohlschlegel JA, Patel DJ, Jacobsen SE Cell. 2014 May 22;157(5):1050-60. doi: 10.1016/j.cell.2014.03.056. PMID:24855943[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhong X, Du J, Hale CJ, Gallego-Bartolome J, Feng S, Vashisht AA, Chory J, Wohlschlegel JA, Patel DJ, Jacobsen SE. Molecular Mechanism of Action of Plant DRM De Novo DNA Methyltransferases. Cell. 2014 May 22;157(5):1050-60. doi: 10.1016/j.cell.2014.03.056. PMID:24855943 doi:http://dx.doi.org/10.1016/j.cell.2014.03.056
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