Summary information and primary citation

PDB-id
7pli; SNAP-derived features in text and JSON formats; DNAproDB
Class
RNA binding protein
Method
X-ray (2.5 Å)
Summary
Dead-box helicase dbpa bound to single stranded RNA and adp-bef3
Reference
Wurm JP (2023): "Structural basis for RNA-duplex unwinding by the DEAD-box helicase DbpA." Rna, 29, 1339-1354. doi: 10.1261/rna.079582.123.
Abstract
DEAD-box RNA helicases are implicated in most aspects of RNA biology, where these enzymes unwind short RNA duplexes in an ATP-dependent manner. During the central step of the unwinding cycle, the two domains of the helicase core form a distinct closed conformation that destabilizes the RNA duplex, which ultimately leads to duplex melting. Despite the importance of this step for the unwinding process no high-resolution structures of this state are available. Here, I used nuclear magnetic resonance spectroscopy and X-ray crystallography to determine structures of the DEAD-box helicase DbpA in the closed conformation, complexed with substrate duplexes and single-stranded unwinding product. These structures reveal that DbpA initiates duplex unwinding by interacting with up to three base-paired nucleotides and a 5' single-stranded RNA duplex overhang. These high-resolution snapshots, together with biochemical assays, rationalize the destabilization of the RNA duplex and are integrated into a conclusive model of the unwinding process.

Cartoon-block schematics in six views (download the tarball)

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