Summary information and primary citation
- PDB-id
-
6uv3;
DSSR-derived features in text and
JSON formats
- Class
- RNA binding protein-RNA
- Method
- X-ray (1.597 Å)
- Summary
- Crystal structure of the core domain of RNA helicase
ddx17 with RNA pri-125a-oligo2
- Reference
-
Ngo TD, Partin AC, Nam Y (2019): "RNA
Specificity and Autoregulation of DDX17, a Modulator of
MicroRNA Biogenesis." Cell Rep,
29, 4024-4035.e5. doi: 10.1016/j.celrep.2019.11.059.
- Abstract
- DDX17, a DEAD-box ATPase, is a multifunctional helicase
important for various RNA functions, including microRNA
maturation. Key questions for DDX17 include how it
recognizes target RNAs and influences their structures, as
well as how its ATPase activity may be regulated. Through
crystal structures and biochemical assays, we show the
ability of the core catalytic domains of DDX17 to recognize
specific sequences in target RNAs. The RNA sequence
preference of the catalytic core is critical for DDX17 to
directly bind and remodel a specific region of primary
microRNAs 3' to the mature sequence, and consequently
enhance processing by Drosha. Furthermore, we identify an
intramolecular interaction between the N-terminal tail
and the DEAD domain of DDX17 to have an autoregulatory role
in controlling the ATPase activity. Thus, we provide the
molecular basis for how cognate RNA recognition and
functional outcomes are linked for DDX17.
