View source for 5af0


==MAEL domain from Bombyx mori Maelstrom==
<StructureSection load='5af0' size='340' side='right'caption='[[5af0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5af0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AF0 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]] 2.401&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5af0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5af0 OCA], [https://pdbe.org/5af0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5af0 RCSB], [https://www.ebi.ac.uk/pdbsum/5af0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5af0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H5AXR2_BOMMO A0A0H5AXR2_BOMMO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Piwi-interacting RNAs (piRNAs) guide Piwi argonautes to their transposon targets for silencing. The highly conserved protein Maelstrom is linked to both piRNA biogenesis and effector roles in this pathway. One defining feature of Maelstrom is the predicted MAEL domain of unknown molecular function. Here, we present the first crystal structure of the MAEL domain from Bombyx Maelstrom, which reveals a nuclease fold. The overall architecture resembles that found in Mg2+- or Mn2+-dependent DEDD nucleases, but a clear distinguishing feature is the presence of a structural Zn2+ ion coordinated by the conserved ECHC residues. Strikingly, metazoan Maelstrom orthologs across the animal kingdom lack the catalytic DEDD residues, and as we show for Bombyx Maelstrom are inactive as nucleases. However, a MAEL domain-containing protein from amoeba having both sequence motifs (DEDD and ECHC) is robustly active as an exoribonuclease. Finally, we show that the MAEL domain of Bombyx Maelstrom displays a strong affinity for single-stranded RNAs. Our studies suggest that the ancient MAEL nuclease domain evolved to function as an RNA-binding module in metazoan Maelstrom.

Metazoan Maelstrom is an RNA-binding protein that has evolved from an ancient nuclease active in protists.,Chen KM, Campbell E, Pandey RR, Yang Z, McCarthy AA, Pillai RS RNA. 2015 Mar 16. PMID:25778731<ref>PMID:25778731</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5af0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bombyx mori]]
[[Category: Large Structures]]
[[Category: Campbell E]]
[[Category: Chen K]]
[[Category: McCarthy AA]]
[[Category: Pandey RR]]
[[Category: Pillai RS]]
[[Category: Yang Z]]