5B16

X-ray structure of DROSHA in complex with the C-terminal tail of DGCR8.

Summary for 5B16

• Entry DOI: 10.2210/pdb5b16/pdb
• Descriptor: Ribonuclease 3,DROSHA,Ribonuclease 3,DROSHA,Ribonuclease 3, Microprocessor complex subunit DGCR8, ZINC ION (3 entities in total)
• Functional Keywords: endonuclease, rnase iii, trimeric complex, zinc finger, hydrolase
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : Q9NRR4 Q8WYQ5
• Total number of polymer chains: 3
• Total formula weight: 118000.68

Authors

Kwon, S.C.,Nguyen, T.A.,Choi, Y.G.,Jo, M.H.,Hohng, S.,Kim, V.N.,Woo, J.S. (deposition date: 2015-11-23, release date: 2016-02-03, Last modification date: 2024-11-20)

Primary citation

Kwon, S.C.,Nguyen, T.A.,Choi, Y.G.,Jo, M.H.,Hohng, S.,Kim, V.N.,Woo, J.S.
Structure of Human DROSHA
Cell, 164:81-90, 2016

PubMed Abstract: MicroRNA maturation is initiated by RNase III DROSHA that cleaves the stem loop of primary microRNA. DROSHA functions together with its cofactor DGCR8 in a heterotrimeric complex known as Microprocessor. Here, we report the X-ray structure of DROSHA in complex with the C-terminal helix of DGCR8. We find that DROSHA contains two DGCR8-binding sites, one on each RNase III domain (RIIID), which mediate the assembly of Microprocessor. The overall structure of DROSHA is surprisingly similar to that of Dicer despite no sequence homology apart from the C-terminal part, suggesting that DROSHA may have evolved from a Dicer homolog. DROSHA exhibits unique features, including non-canonical zinc-finger motifs, a long insertion in the first RIIID, and the kinked link between Connector helix and RIIID, which explains the 11-bp-measuring "ruler" activity of DROSHA. Our study implicates the evolutionary origin of DROSHA and elucidates the molecular basis of Microprocessor assembly and primary microRNA processing.

PubMed: 26748718
DOI: 10.1016/j.cell.2015.12.019

Experimental method

X-RAY DIFFRACTION (3.2 Å)