期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 59, 期 7, 页码 2837-2843出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201912522
关键词
magnesium; oligonucleotides; reaction mechanisms; RNA; structure-function relationships
资金
- Austrian Science Fund FWF [P27947, P31691, M2517]
- Austrian Research Promotion Agency FFG (West-Austrian BioNMR) [858017]
- NIH [1U19CA179564]
- NIH (Cancer Center Core Grant) [P30CA008748]
- Natural Science Foundation of China [91640104, 31670826, 31870810]
- outstanding youth fund of Zhejiang Province [LR19C050003]
- Fundamental Research Funds for the Central Universities [2017QN81010]
- Zhejiang University
- Austrian Science Fund (FWF) [P31691, P27947, M2517] Funding Source: Austrian Science Fund (FWF)
Pistol ribozymes constitute a new class of small self-cleaving RNAs. Crystal structures have been solved, providing three-dimensional snapshots along the reaction coordinate of pistol phosphodiester cleavage, corresponding to the pre-catalytic state, a vanadate mimic of the transition state, and the product. The results led to the proposed underlying chemical mechanism. Importantly, a hydrated Mg2+ ion remains innersphere-coordinated to N7 of G33 in all three states, and is consistent with its likely role as acid in general acid base catalysis (delta and beta catalysis). Strikingly, the new structures shed light on a second hydrated Mg2+ ion that approaches the scissile phosphate from its binding site in the pre-cleavage state to reach out for water-mediated hydrogen bonding in the cyclophosphate product. The major role of the second Mg2+ ion appears to be the stabilization of product conformation. This study delivers a mechanistic understanding of ribozyme-catalyzed backbone cleavage.
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