6V5B

Human Drosha and DGCR8 in complex with Primary MicroRNA (MP/RNA complex) - Active state

Summary for 6V5B

• Entry DOI: 10.2210/pdb6v5b/pdb
• EMDB information: 21051
• Descriptor: Ribonuclease 3, Microprocessor complex subunit DGCR8, Pri-miR-16-2 (78-MER), ... (5 entities in total)
• Functional Keywords: microprocessor, drosha, dgcr8, primary microrna, rna binding protein, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 273298.76

Authors

Partin, A.,Zhang, K.,Jeong, B.,Herrell, E.,Li, S.,Chiu, W.,Nam, Y. (deposition date: 2019-12-04, release date: 2020-04-08, Last modification date: 2024-03-06)

Primary citation

Partin, A.C.,Zhang, K.,Jeong, B.C.,Herrell, E.,Li, S.,Chiu, W.,Nam, Y.
Cryo-EM Structures of Human Drosha and DGCR8 in Complex with Primary MicroRNA.
Mol.Cell, 78:411-, 2020

PubMed Abstract: Metazoan microRNAs require specific maturation steps initiated by Microprocessor, comprising Drosha and DGCR8. Lack of structural information for the assembled complex has hindered an understanding of how Microprocessor recognizes primary microRNA transcripts (pri-miRNAs). Here we present a cryoelectron microscopy structure of human Microprocessor with a pri-miRNA docked in the active site, poised for cleavage. The basal junction is recognized by a four-way intramolecular junction in Drosha, triggered by the Belt and Wedge regions that clamp over the ssRNA. The belt is important for efficiency and accuracy of pri-miRNA processing. Two dsRBDs form a molecular ruler to measure the stem length between the two dsRNA-ssRNA junctions. The specific organization of the dsRBDs near the apical junction is independent of Drosha core domains, as observed in a second structure in the partially docked state. Collectively, we derive a molecular model to explain how Microprocessor recognizes a pri-miRNA and accurately identifies the cleavage site.

PubMed: 32220646
DOI: 10.1016/j.molcel.2020.02.016

Experimental method

ELECTRON MICROSCOPY (3.7 Å)