8VX8
Cryo-EM Structure of DHX36 bound to the cMyc DNA G-quadruplex, Class 1
Summary for 8VX8
| Entry DOI | 10.2210/pdb8vx8/pdb |
| EMDB information | 43612 |
| Descriptor | ATP-dependent DNA/RNA helicase DHX36, DNA (29-MER) (2 entities in total) |
| Functional Keywords | deah-box helicase, helicase, g-quadruplex, rna, motor protein |
| Biological source | Bos taurus (cattle) More |
| Total number of polymer chains | 3 |
| Total formula weight | 129886.60 |
| Authors | |
| Primary citation | Banco, M.T.,Paul, T.,Jiang, J.,Myong, S.,Ferre-D'Amare, A.R. Structural basis for dual DNA and RNA specificity of the G-quadruplex-resolving DEAH-box helicase DHX36. Cell Rep, 44:116136-116136, 2025 Cited by PubMed Abstract: DEAH-box helicases, which share a structurally conserved ATPase core, function in all facets of eukaryotic gene expression. While most helicases are highly specialized for their substrates, DHX36 (DEAH-box helicase 36) resolves both DNA and RNA G-quadruplexes. To elucidate the molecular basis of this versatility, we have determined cryo-electron microscopy structures of bovine DHX36 bound to a three-tier RNA G-quadruplex and a six-tier DNA G-quadruplex at 2.6 and 3.4 Å resolution, respectively. Kinetic and smFRET characterizations of structure-guided mutants indicate a key role for the RecA2 domain of the helicase core in DNA vs. RNA discrimination. Furthermore, our structures show that a sequence-divergent RecA2 domain surface loop synergizes with a DHX36-specific N-terminal extension to orthogonally recognize features that specify G-quadruplexes over other nucleic acid structures. Our analysis suggests that recognizing their folded substrates by DEAH-box helicases may generally involve ornamentations of their structural cores acting synergistically with specialized peripheral elements. PubMed: 40833853DOI: 10.1016/j.celrep.2025.116136 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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