6HYT
Crystal structure of DHX8 helicase domain bound to ADP at 2.3 Angstrom
Summary for 6HYT
| Entry DOI | 10.2210/pdb6hyt/pdb |
| Descriptor | ATP-dependent RNA helicase DHX8, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (8 entities in total) |
| Functional Keywords | helicase, splicing, rna, rna binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 311383.25 |
| Authors | Felisberto-Rodrigues, C.,Thomas, J.C.,McAndrew, P.C.,Le Bihan, Y.V.,Burke, R.,Workman, P.,van Montfort, R.L.M. (deposition date: 2018-10-22, release date: 2019-08-28, Last modification date: 2024-05-15) |
| Primary citation | Felisberto-Rodrigues, C.,Thomas, J.C.,McAndrew, C.,Le Bihan, Y.V.,Burke, R.,Workman, P.,van Montfort, R.L.M. Structural and functional characterisation of human RNA helicase DHX8 provides insights into the mechanism of RNA-stimulated ADP release. Biochem.J., 476:2521-2543, 2019 Cited by PubMed Abstract: DHX8 is a crucial DEAH-box RNA helicase involved in splicing and required for the release of mature mRNA from the spliceosome. Here, we report the biochemical characterisation of full-length human DHX8 and the catalytically active helicase core DHX8Δ547, alongside crystal structures of DHX8Δ547 bound to ADP and a structure of DHX8Δ547 bound to poly(A) single-strand RNA. Our results reveal that DHX8 has an binding preference for adenine-rich RNA and that RNA binding triggers the release of ADP through significant conformational flexibility in the conserved DEAH-, P-loop and hook-turn motifs. We demonstrate the importance of R620 and both the hook-turn and hook-loop regions for DHX8 helicase activity and propose that the hook-turn acts as a gatekeeper to regulate the directional movement of the 3' end of RNA through the RNA-binding channel. This study provides an in-depth understanding of the activity of DHX8 and contributes insights into the RNA-unwinding mechanisms of the DEAH-box helicase family. PubMed: 31409651DOI: 10.1042/BCJ20190383 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.33 Å) |
Structure validation
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