2xdy | pdb_00002xdy

CRYSTAL STRUCTURE OF THE N. CRASSA QDE-2 AGO MID DOMAIN

spinqualitylabelsall models 2xdy, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xdy is a 1 chain structure with sequence from Chrysonilia crassa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Argonaute (AGO) proteins are core components of RNA-induced silencing complexes and have essential roles in RNA-mediated gene silencing. They are characterized by a bilobal architecture, consisting of one lobe containing the amino-terminal and PAZ domains and another containing the MID and PIWI domains. Except for the PAZ domain, structural information on eukaryotic AGO domains is not yet available. In this study, we report the crystal structure of the MID domain of the eukaryotic AGO protein QDE-2 from Neurospora crassa. This domain adopts a Rossmann-like fold and recognizes the 5'-terminal nucleotide of a guide RNA in a manner similar to its prokaryotic counterparts. The 5'-nucleotide-binding site shares common residues with a second, adjacent ligand-binding site, suggesting a mechanism for the cooperative binding of ligands to the MID domain of eukaryotic AGOs. Crystal structure and ligand binding of the MID domain of a eukaryotic Argonaute protein.,Boland A, Tritschler F, Heimstadt S, Izaurralde E, Weichenrieder O EMBO Rep. 2010 Jul;11(7):522-7. Epub 2010 Jun 11. PMID:20539312 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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