Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6O16

Crystal structure of murine DHX37 in complex with RNA

Summary for 6O16
Entry DOI10.2210/pdb6o16/pdb
DescriptorDEAH (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 Keywordsrna helicase, ribosome biogenesis, rna-dependent atpase, hydrolase-rna complex, hydrolase/rna
Biological sourceMus musculus (Mouse)
More
Total number of polymer chains4
Total formula weight223464.35
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 citationBoneberg, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.875 Å)
Structure validation

238582

数据于2025-07-09公开中

PDB statisticsPDBj update infoContact PDBjnumon