6O16

Crystal structure of murine DHX37 in complex with RNA

Summary for 6O16

• Entry DOI: 10.2210/pdb6o16/pdb
• Descriptor: DEAH (Asp-Glu-Ala-His) box polypeptide 37, RNA (5'-R(*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3') (2 entities in total)
• Functional Keywords: rna helicase, ribosome biogenesis, rna-dependent atpase, hydrolase-rna complex, hydrolase/rna
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 4
• Total formula weight: 223464.35

Authors

Boneberg, F.,Brandmann, T.,Kobel, L.,van den Heuvel, J.,Bargsten, K.,Bammert, L.,Kutay, U.,Jinek, M. (deposition date: 2019-02-18, release date: 2019-04-17, Last modification date: 2024-03-13)

Primary citation

Boneberg, F.M.,Brandmann, T.,Kobel, L.,van den Heuvel, J.,Bargsten, K.,Bammert, L.,Kutay, U.,Jinek, M.
Molecular mechanism of the RNA helicase DHX37 and its activation by UTP14A in ribosome biogenesis.
Rna, 25:685-701, 2019

PubMed Abstract: Eukaryotic ribosome biogenesis is a highly orchestrated process involving numerous assembly factors including ATP-dependent RNA helicases. The DEAH helicase DHX37 (Dhr1 in yeast) is activated by the ribosome biogenesis factor UTP14A to facilitate maturation of the small ribosomal subunit. We report the crystal structure of DHX37 in complex with single-stranded RNA, revealing a canonical DEAH ATPase/helicase architecture complemented by a structurally unique carboxy-terminal domain (CTD). Structural comparisons of the nucleotide-free DHX37-RNA complex with DEAH helicases bound to RNA and ATP analogs reveal conformational changes resulting in a register shift in the bound RNA, suggesting a mechanism for ATP-dependent 3'-5' RNA translocation. We further show that a conserved sequence motif in UTP14A interacts with and activates DHX37 by stimulating its ATPase activity and enhancing RNA binding. In turn, the CTD of DHX37 is required, but not sufficient, for interaction with UTP14A in vitro and is essential for ribosome biogenesis in vivo. Together, these results shed light on the mechanism of DHX37 and the function of UTP14A in controlling its recruitment and activity during ribosome biogenesis.

PubMed: 30910870
DOI: 10.1261/rna.069609.118

Experimental method

X-RAY DIFFRACTION (2.875 Å)