6OIT
CryoEM structure of Arabidopsis DDR' complex (DRD1 peptide-DMS3-RDM1)
Summary for 6OIT
| Entry DOI | 10.2210/pdb6oit/pdb |
| EMDB information | 20081 |
| Descriptor | Protein RDM1, Protein DEFECTIVE IN MERISTEM SILENCING 3, Protein CHROMATIN REMODELING 35 (3 entities in total) |
| Functional Keywords | smc-hinge, coiled-coil, snf2, rna-directed dna methylation, plant protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
| Total number of polymer chains | 7 |
| Total formula weight | 247346.04 |
| Authors | Wongpalee, S.P.,Liu, S.,Zhou, Z.H.,Jacobsen, S.E. (deposition date: 2019-04-09, release date: 2019-07-24, Last modification date: 2024-03-20) |
| Primary citation | Wongpalee, S.P.,Liu, S.,Gallego-Bartolome, J.,Leitner, A.,Aebersold, R.,Liu, W.,Yen, L.,Nohales, M.A.,Kuo, P.H.,Vashisht, A.A.,Wohlschlegel, J.A.,Feng, S.,Kay, S.A.,Zhou, Z.H.,Jacobsen, S.E. CryoEM structures of Arabidopsis DDR complexes involved in RNA-directed DNA methylation. Nat Commun, 10:3916-3916, 2019 Cited by PubMed Abstract: Transcription by RNA polymerase V (Pol V) in plants is required for RNA-directed DNA methylation, leading to transcriptional gene silencing. Global chromatin association of Pol V requires components of the DDR complex DRD1, DMS3 and RDM1, but the assembly process of this complex and the underlying mechanism for Pol V recruitment remain unknown. Here we show that all DDR complex components co-localize with Pol V, and we report the cryoEM structures of two complexes associated with Pol V recruitment-DR (DMS3-RDM1) and DDR' (DMS3-RDM1-DRD1 peptide), at 3.6 Å and 3.5 Å resolution, respectively. RDM1 dimerization at the center frames the assembly of the entire complex and mediates interactions between DMS3 and DRD1 with a stoichiometry of 1 DRD1:4 DMS3:2 RDM1. DRD1 binding to the DR complex induces a drastic movement of a DMS3 coiled-coil helix bundle. We hypothesize that both complexes are functional intermediates that mediate Pol V recruitment. PubMed: 31477705DOI: 10.1038/s41467-019-11759-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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