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| | ==Crystal structure of Arabidopsis DDL FHA domain== | | ==Crystal structure of Arabidopsis DDL FHA domain== |
| - | <StructureSection load='3vpy' size='340' side='right' caption='[[3vpy]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3vpy' size='340' side='right'caption='[[3vpy]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vpy]] is a 1 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=3VPY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VPY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vpy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VPY FirstGlance]. <br> |
| | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDL, At3g20550, K10D20.9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDL, At3g20550, K10D20.9 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=3vpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpy OCA], [http://pdbe.org/3vpy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vpy RCSB], [http://www.ebi.ac.uk/pdbsum/3vpy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vpy 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=3vpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpy OCA], [https://pdbe.org/3vpy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vpy RCSB], [https://www.ebi.ac.uk/pdbsum/3vpy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vpy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DDL_ARATH DDL_ARATH]] Involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. May facilitate DCL1 to access or recognize primary miRNAs. Binds RNA non-specifically.<ref>PMID:18632581</ref> | + | [[https://www.uniprot.org/uniprot/DDL_ARATH DDL_ARATH]] Involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. May facilitate DCL1 to access or recognize primary miRNAs. Binds RNA non-specifically.<ref>PMID:18632581</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Arath]] | | [[Category: Arath]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Machida, S]] | | [[Category: Machida, S]] |
| | [[Category: Yuan, Y A]] | | [[Category: Yuan, Y A]] |
| Structural highlights
Function
[DDL_ARATH] Involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. May facilitate DCL1 to access or recognize primary miRNAs. Binds RNA non-specifically.[1]
Publication Abstract from PubMed
Dawdle (DDL) is a microRNA processing protein essential for the development of Arabidopsis. DDL contains a putative nuclear localization signal at its amino terminus and forkhead-associated (FHA) domain at the carboxyl terminus. Here we report the crystal structure of FHA domain of Arabidopsis Dawdle, determined by multiple-wavelength anomalous dispersion method at 1.7 A resolution. DDL FHA structure displays a seven-stranded beta-sandwich architecture that contains a unique structural motif comprising two long anti-parallel strands. Strikingly, crystal packing of DDL FHA domain reveals that a glutamate residue from the symmetry-related DDL FHA domain, a structural mimic of the phospho-threonine, is specifically recognized by the structurally conserved phospho-threonine binding cleft. Consistent with the structural observations, co-immuno-precipitation experiments performed in N. benthamiana show that DDL FHA domain co-immuno-precipitates with DCL1 fragments containing the predicted pThr+3(Ile/Val/Leu/Asp) motif. Taken together, we count the recognition of the target residue by the canonical binding cleft of DDL FHA domain as the key molecular event to instate FHA domain-mediated protein-protein interaction in plant miRNA processing.
Crystal Structure of Arabidopsis thaliana Dawdle Forkhead-Associated Domain reveals a conserved phospho-threonine recognition cleft for Dicer-like1 binding.,Machida S, Yuan AY Mol Plant. 2013 Jan 11. PMID:23313986[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yu B, Bi L, Zheng B, Ji L, Chevalier D, Agarwal M, Ramachandran V, Li W, Lagrange T, Walker JC, Chen X. The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act in small RNA biogenesis. Proc Natl Acad Sci U S A. 2008 Jul 22;105(29):10073-8. doi:, 10.1073/pnas.0804218105. Epub 2008 Jul 15. PMID:18632581 doi:http://dx.doi.org/10.1073/pnas.0804218105
- ↑ Machida S, Yuan AY. Crystal Structure of Arabidopsis thaliana Dawdle Forkhead-Associated Domain reveals a conserved phospho-threonine recognition cleft for Dicer-like1 binding. Mol Plant. 2013 Jan 11. PMID:23313986 doi:http://dx.doi.org/10.1093/mp/sst007
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