8VX8

Cryo-EM Structure of DHX36 bound to the cMyc DNA G-quadruplex, Class 1

8VX8 の概要

• エントリーDOI: 10.2210/pdb8vx8/pdb
• EMDBエントリー: 43612
• 分子名称: ATP-dependent DNA/RNA helicase DHX36, DNA (29-MER) (2 entities in total)
• 機能のキーワード: deah-box helicase, helicase, g-quadruplex, rna, motor protein
• 由来する生物種: Bos taurus (cattle); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 129886.60

構造登録者

Banco, M.T.,Ferre-D'Amare, A.R. (登録日: 2024-02-03, 公開日: 2025-09-03)

主引用文献

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

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: 40833853
DOI: 10.1016/j.celrep.2025.116136

実験手法

ELECTRON MICROSCOPY (3.4 Å)