5af0

MAEL domain from Bombyx mori Maelstrom

spinqualitylabelsall models 5af0, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5af0 is a 4 chain structure with sequence from Bombyx mori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.401Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H5AXR2_BOMMO 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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