7BBB
Solution structure of C-terminal RecA and RRM domains of the DEAD box helicase DbpA
Summary for 7BBB
| Entry DOI | 10.2210/pdb7bbb/pdb |
| NMR Information | BMRB: 34584 |
| Descriptor | ATP-dependent RNA helicase DbpA (1 entity in total) |
| Functional Keywords | dead box helicase, ribosome biogenesis, rna, rna binding protein |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 1 |
| Total formula weight | 27014.06 |
| Authors | Wurm, J.P.,Sprangers, R. (deposition date: 2020-12-17, release date: 2021-07-14, Last modification date: 2024-06-19) |
| Primary citation | Wurm, J.P.,Glowacz, K.A.,Sprangers, R. Structural basis for the activation of the DEAD-box RNA helicase DbpA by the nascent ribosome. Proc.Natl.Acad.Sci.USA, 118:-, 2021 Cited by PubMed Abstract: The adenosine triphosphate (ATP)-dependent DEAD-box RNA helicase DbpA from functions in ribosome biogenesis. DbpA is targeted to the nascent 50S subunit by an ancillary, carboxyl-terminal RNA recognition motif (RRM) that specifically binds to hairpin 92 (HP92) of the 23S ribosomal RNA (rRNA). The interaction between HP92 and the RRM is required for the helicase activity of the RecA-like core domains of DbpA. Here, we elucidate the structural basis by which DbpA activity is endorsed when the enzyme interacts with the maturing ribosome. We used nuclear magnetic resonance (NMR) spectroscopy to show that the RRM and the carboxyl-terminal RecA-like domain tightly interact. This orients HP92 such that this RNA hairpin can form electrostatic interactions with a positively charged patch in the N-terminal RecA-like domain. Consequently, the enzyme can stably adopt the catalytically important, closed conformation. The substrate binding mode in this complex reveals that a region 5' to helix 90 in the maturing ribosome is specifically targeted by DbpA. Finally, our results indicate that the ribosome maturation defects induced by a dominant negative DbpA mutation are caused by a delayed dissociation of DbpA from the nascent ribosome. Taken together, our findings provide unique insights into the important regulatory mechanism that modulates the activity of DbpA. PubMed: 34453003DOI: 10.1073/pnas.2105961118 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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