3vpy
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3vpy is ON HOLD Authors: Yuan, Y. A., Machida, S. Description: Crystal structure of Arabidopsis DDL FHA domain) |
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of Arabidopsis DDL FHA domain== | |
+ | <StructureSection load='3vpy' size='340' side='right'caption='[[3vpy]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3vpy]] is a 1 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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> | ||
+ | == Function == | ||
+ | [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;"> | ||
+ | == 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<ref>PMID:23313986</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 3vpy" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Arabidopsis thaliana]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Machida S]] | ||
+ | [[Category: Yuan YA]] |
Current revision
Crystal structure of Arabidopsis DDL FHA domain
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