7W82
Crystal structure of maize RDR2
Summary for 7W82
| Entry DOI | 10.2210/pdb7w82/pdb |
| Descriptor | RNA-dependent RNA polymerase (1 entity in total) |
| Functional Keywords | rdr2, rddm, rna polymerase, plant protein |
| Biological source | Zea mays |
| Total number of polymer chains | 1 |
| Total formula weight | 115392.17 |
| Authors | |
| Primary citation | Du, X.,Yang, Z.,Ariza, A.J.F.,Wang, Q.,Xie, G.,Li, S.,Du, J. Structure of plant RNA-DEPENDENT RNA POLYMERASE 2, an enzyme involved in small interfering RNA production. Plant Cell, 34:2140-2149, 2022 Cited by PubMed Abstract: In plants, the biogenesis of small interfering RNA (siRNA) requires a family of RNA-dependent RNA polymerases that convert single-stranded RNA (ssRNA) into double-stranded RNA (dsRNA), which is subsequently cleaved into defined lengths by Dicer endonucleases. Here, we determined the structure of maize (Zea mays) RNA-DEPENDENT RNA POLYMERASE 2 (ZmRDR2) in the closed and open conformations. The core catalytic region of ZmRDR2 possesses the canonical DNA-dependent RNA polymerase (DdRP) catalytic sites, pointing to a shared RNA production mechanism between DdRPs and plant RDR-family proteins. Apo-ZmRDR2 adopts a highly compact structure, representing an inactive closed conformation. By contrast, adding RNA induced a significant conformational change in the ZmRDR2 Head domain that opened the RNA binding tunnel, suggesting this is an active elongation conformation of ZmRDR2. Overall, our structural studies trapped both the active and inactive conformations of ZmRDR2, providing insights into the molecular mechanism of dsRNA synthesis during plant siRNA production. PubMed: 35188193DOI: 10.1093/plcell/koac067 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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