6UV2
Crystal structure of the core domain of RNA helicase DDX17 with RNA pri-125a-oligo1
Summary for 6UV2
Entry DOI | 10.2210/pdb6uv2/pdb |
Descriptor | Probable ATP-dependent RNA helicase DDX17, RNA 125a_oligo1, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total) |
Functional Keywords | dead-box atpase, rna helicase, rna binding, rna binding protein, rna binding protein-rna complex, rna binding protein/rna |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 2 |
Total formula weight | 55006.01 |
Authors | Ngo, T.D.,Partin, A.C.,Nam, Y. (deposition date: 2019-11-01, release date: 2020-01-01, Last modification date: 2024-04-03) |
Primary citation | Ngo, T.D.,Partin, A.C.,Nam, Y. RNA Specificity and Autoregulation of DDX17, a Modulator of MicroRNA Biogenesis. Cell Rep, 29:4024-4035.e5, 2019 Cited by PubMed 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. PubMed: 31851931DOI: 10.1016/j.celrep.2019.11.059 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.894 Å) |
Structure validation
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