Crystal structure and ligand binding of the MID domain of a eukaryotic Argonaute protein
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- Andreas Boland
- Department of Biochemistry, Max Planck Institute for Developmental Biology Spemannstrasse 35 Tübingen D‐72076 Germany
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- Felix Tritschler
- Department of Biochemistry, Max Planck Institute for Developmental Biology Spemannstrasse 35 Tübingen D‐72076 Germany
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- Susanne Heimstädt
- Department of Biochemistry, Max Planck Institute for Developmental Biology Spemannstrasse 35 Tübingen D‐72076 Germany
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- Elisa Izaurralde
- Department of Biochemistry, Max Planck Institute for Developmental Biology Spemannstrasse 35 Tübingen D‐72076 Germany
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- Oliver Weichenrieder
- Department of Biochemistry, Max Planck Institute for Developmental Biology Spemannstrasse 35 Tübingen D‐72076 Germany
抄録
<jats:p>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 <jats:italic>Neurospora crassa.</jats:italic> 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.</jats:p>
収録刊行物
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- EMBO reports
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EMBO reports 11 (7), 522-527, 2010-06-11
Springer Science and Business Media LLC
