2XDY
Crystal structure of the N. crassa QDE-2 AGO MID domain
Summary for 2XDY
| Entry DOI | 10.2210/pdb2xdy/pdb |
| Descriptor | POST-TRANSCRIPTIONAL GENE SILENCING PROTEIN QDE-2, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | argonaute, gene silencing, rna-induced silencing complex, 5' end binding, rossmann-like fold, rna binding protein |
| Biological source | NEUROSPORA CRASSA |
| Total number of polymer chains | 1 |
| Total formula weight | 16263.00 |
| Authors | Boland, A.,Tritschler, F.,Weichenrieder, O. (deposition date: 2010-05-10, release date: 2010-06-16, Last modification date: 2024-05-08) |
| Primary citation | Boland, A.,Tritschler, F.,Heimstaedt, S.,Izaurralde, E.,Weichenrieder, O. Crystal Structure and Ligand Binding of the Mid Domain of a Eukaryotic Argonaute Protein. Embo Rep., 11:522-, 2010 Cited by PubMed Abstract: 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. PubMed: 20539312DOI: 10.1038/EMBOR.2010.81 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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