6LXD

Pri-miRNA bound DROSHA-DGCR8 complex

Summary for 6LXD

• Entry DOI: 10.2210/pdb6lxd/pdb
• EMDB information: 30005
• Descriptor: Ribonuclease 3, Microprocessor complex subunit DGCR8, RNA (102-mer), ... (4 entities in total)
• Functional Keywords: ribonuclease, rna binding protein, hydrolase-rna binding protein-rna complex, hydrolase/rna binding protein/rna
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 320623.20

Authors

Jin, W.,Wang, J.,Liu, C.P.,Wang, H.W.,Xu, R.M. (deposition date: 2020-02-10, release date: 2020-04-15, Last modification date: 2024-03-27)

Primary citation

Jin, W.,Wang, J.,Liu, C.P.,Wang, H.W.,Xu, R.M.
Structural Basis for pri-miRNA Recognition by Drosha.
Mol.Cell, 78:423-, 2020

PubMed Abstract: A commencing and critical step in miRNA biogenesis involves processing of pri-miRNAs in the nucleus by Microprocessor. An important, but not completely understood, question is how Drosha, the catalytic subunit of Microprocessor, binds pri-miRNAs and correctly specifies cleavage sites. Here we report the cryoelectron microscopy structures of the Drosha-DGCR8 complex with and without a pri-miRNA. The RNA-bound structure provides direct visualization of the tertiary structure of pri-miRNA and shows that a helix hairpin in the extended PAZ domain and the mobile basic (MB) helix in the RNase IIIa domain of Drosha coordinate to recognize the single-stranded to double-stranded junction of RNA, whereas the dsRNA binding domain makes extensive contacts with the RNA stem. Furthermore, the RNA-free structure reveals an autoinhibitory conformation of the PAZ helix hairpin. These findings provide mechanistic insights into pri-miRNA cleavage site selection and conformational dynamics governing pri-miRNA recognition by the catalytic component of Microprocessor.

PubMed: 32220645
DOI: 10.1016/j.molcel.2020.02.024

Experimental method

ELECTRON MICROSCOPY (3.9 Å)