Scientists have shown for the first time an accurate atomic model of the RNA-cut molecular clock

Beijing, December 3 (Reporter Deng Wei) West Lake University School of Life Sciences Professor Shi Yigong research group entitled "ATP hydrolyzed enzyme / deconstructive enzyme Prp2 and its activation factor Sp2 catalytic shear activation process of structural remodeling molecular structure", published in the journal Science on November 27 in a long text. This paper reports on the high-resolution electromirror structure of the shear body 2.5 E, which is currently reported to be the highest resolution of the shear structure, and for the first time shows the "power-driven" protein -ATP hydrolyzedase/deconstructive enzyme Prp2 and its activation factor Sppe2, which catalyzes the structural basis of its remodeling, providing the clearest structural information to date for understanding the molecular structure of the shear activation remodeling. Studies have shown that more than 95% of human genes will have RNA shearing, any abnormal, wrong RNA shearing, will lead to serious genetic disorders and diseases, currently about 35% of human genetic diseases are related to RNA shear abnormalities, for these RNA shearing drug targets to design drugs, is expected to promote the treatment of some human diseases.
behavior, language, thinking and other life activities of living organisms are controlled by genes, and RNA cutting is one of the important links in the regulation of gene expression in ceuteral organisms. The person responsible for performing the RNA shear reaction is the shear body in the nuclei of the cell, and the shear body needs the "power-driven" protein - ATP hydrolyzed enzyme / de-cyclonease for strict regulation, they in catalytic shear body composition changes, control the process of RNA shearing, RNA testing and proofreading process plays an extremely critical role, known as RNA cutting "molecular clock."
2015, shi's team first reported on the high-resolution structure of the cleavage yeast shear 3.6 E in the world, and for the first time demonstrated the structure of the near-atomic resolution of the catalytic center of the shear. However, how to explain the molecular process of the shear reshaping protein to control the transition of the state of the shear body and reveal the precise atomic model of RNA cutting "molecular clock" has always been one of the core problems in the field.
The research team reconstructed the structure of the Bactcomplex frozen electromirror with a total resolution of 2.5 E using single-particle cryomirscopy technology, in which the structural remodeling protein ATP hydrolyzing enzyme/deconstructive enzyme Prp2 and its activation factor Spp2 at the edge of the shear body had a resolution of up to 3.2 E, and constructed an atomic model. At such a high resolution, the analyzedBactcomplex structure for the first time observed water molecules in the core region of the shear body using hydrogen bonds to participate in the identification of critical shearing points and to bind to metal ions. Surprisingly, the structure shows that the activation factor Sp2 secures Prp2 to the clip body through four key anchor anchor points. Spp2's important role in activating the sp clip and catalytic shear structural remodeling for Prp2 has also been verified by a large number of bio-chemical experiments based on structural design.