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- W4362696923 abstract "Helicases are motor enzymes found in every living organism and viruses, where they maintain the stability of the genome and control against false recombination. The DEAH-box helicase Prp43 plays a crucial role in pre-mRNA splicing in unicellular organisms by translocating single-stranded RNA. The molecular mechanisms and conformational transitions of helicases are not understood at the atomic level. We present a complete conformational cycle of RNA translocation by Prp43 in atomic detail based on molecular dynamics simulations. To enable the sampling of such complex transition on the millisecond timescale, we combined two enhanced sampling techniques, namely simulated tempering and adaptive sampling guided by crystallographic data. During RNA translocation, the center-of-mass motions of the RecA-like domains followed the established inchworm model, whereas the domains crawled along the RNA in a caterpillar-like movement, suggesting an inchworm/caterpillar model. However, this crawling required a complex sequence of atomic-scale transitions involving the release of an arginine finger from the ATP pocket, stepping of the hook-loop and hook-turn motifs along the RNA backbone, and several others. These findings highlight that large-scale domain dynamics may be controlled by complex sequences of atomic-scale transitions." @default.
- W4362696923 created "2023-04-09" @default.
- W4362696923 creator A5068002595 @default.
- W4362696923 creator A5086212875 @default.
- W4362696923 date "2023-04-07" @default.
- W4362696923 modified "2023-10-17" @default.
- W4362696923 title "Continuous millisecond conformational cycle of a DEAH box helicase reveals control of domain motions by atomic-scale transitions" @default.
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- W4362696923 doi "https://doi.org/10.1038/s42003-023-04751-z" @default.
- W4362696923 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37029280" @default.
- W4362696923 hasPublicationYear "2023" @default.
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- W4362696923 hasAuthorship W4362696923A5068002595 @default.
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