Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis of RNA-induced autoregulation of the DExH-type RNA helicase maleless.
Journal, issue, pages	Mol Cell, Vol. 83, Issue 23, Page 4318-4333.e10, Year 2023
Publish date	Dec 7, 2023
Authors	Pravin Kumar Ankush Jagtap / Marisa Müller / Anna E Kiss / Andreas W Thomae / Karine Lapouge / Martin Beck / Peter B Becker / Janosch Hennig /
PubMed Abstract	RNA unwinding by DExH-type helicases underlies most RNA metabolism and function. It remains unresolved if and how the basic unwinding reaction of helicases is regulated by auxiliary domains. We ...RNA unwinding by DExH-type helicases underlies most RNA metabolism and function. It remains unresolved if and how the basic unwinding reaction of helicases is regulated by auxiliary domains. We explored the interplay between the RecA and auxiliary domains of the RNA helicase maleless (MLE) from Drosophila using structural and functional studies. We discovered that MLE exists in a dsRNA-bound open conformation and that the auxiliary dsRBD2 domain aligns the substrate RNA with the accessible helicase tunnel. In an ATP-dependent manner, dsRBD2 associates with the helicase module, leading to tunnel closure around ssRNA. Furthermore, our structures provide a rationale for blunt-ended dsRNA unwinding and 3'-5' translocation by MLE. Structure-based MLE mutations confirm the functional relevance of our model for RNA unwinding. Our findings contribute to our understanding of the fundamental mechanics of auxiliary domains in DExH helicase MLE, which serves as a model for its human ortholog and potential therapeutic target, DHX9/RHA.
External links	Mol Cell / PubMed:37989319
Methods	EM (single particle)
Resolution	2.86 - 4.24 Å
Structure data	15931 8b9g EMDB-15931, PDB-8b9g: Cryo-EM structure of MLE in complex with ADP:AlF4 and U10 RNA Method: EM (single particle) / Resolution: 2.86 Å 15932 8b9i EMDB-15932, PDB-8b9i: Cryo-EM structure of MLE in complex with ADP:AlF4 and UUC RNA Method: EM (single particle) / Resolution: 2.95 Å 15933 8b9j EMDB-15933, PDB-8b9j: Cryo-EM structure of MLE in complex with ADP:AlF4 Method: EM (single particle) / Resolution: 3.45 Å 15934 8b9k EMDB-15934, PDB-8b9k: Cryo-EM structure of MLE in complex with ADP:AlF4 and SL7modUUC RNA Method: EM (single particle) / Resolution: 4.04 Å 15935 8b9l EMDB-15935, PDB-8b9l: Cryo-EM structure of MLE Method: EM (single particle) / Resolution: 3.45 Å 17703 8pjb EMDB-17703, PDB-8pjb: Cryo-EM structure of MLE in complex with UUC RNA and ADP Method: EM (single particle) / Resolution: 3.62 Å 17711 8pjj EMDB-17711, PDB-8pjj: Cryo-EM structure of MLE in complex with SL7UUC RNA and ADP Method: EM (single particle) / Resolution: 4.24 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-ALF: TETRAFLUOROALUMINATE ION ChemComp-HOH: WATER ChemComp-MG*: Unknown entry
Source	drosophila melanogaster (fruit fly)
Keywords	RNA BINDING PROTEIN / RNA Helicase / Drosophila dosage compensation