7w59

The cryo-EM structure of human pre-C*-I complex

spinqualitylabelsall models 7w59, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7w59 is a 10 chain structure with sequence from Homo sapiens and Unidentified adenovirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.6Å Ligands: ATP, GTP, IHP, MG, SEP, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease PRP8_HUMAN Defects in PRPF8 are the cause of retinitis pigmentosa type 13 (RP13) [MIM:600059. RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP13 inheritance is autosomal dominant. [:] Function PRP8_HUMAN Central component of the spliceosome, which may play a role in aligning the pre-mRNA 5'- and 3'-exons for ligation. Interacts with U5 snRNA, and with pre-mRNA 5'-splice sites in B spliceosomes and 3'-splice sites in C spliceosomes. Publication Abstract from PubMed Pre-mRNA splicing involves two sequential reactions: branching and exon ligation. The C complex after branching undergoes remodeling to become the C( *) complex, which executes exon ligation. Here, we report cryo-EM structures of two intermediate human spliceosomal complexes, pre-C( *)-I and pre-C( *)-II, both at 3.6 A. In both structures, the 3' splice site is already docked into the active site, the ensuing 3' exon sequences are anchored on PRP8, and the step II factor FAM192A contacts the duplex between U2 snRNA and the branch site. In the transition of pre-C( *)-I to pre-C( *)-II, the step II factors Cactin, FAM32A, PRKRIP1, and SLU7 are recruited. Notably, the RNA helicase PRP22 is positioned quite differently in the pre-C( *)-I, pre-C( *)-II, and C( *) complexes, suggesting a role in 3' exon binding and proofreading. Together with information on human C and C( *) complexes, our studies recapitulate a molecular choreography of the C-to-C( *) transition, revealing mechanistic insights into exon ligation. Mechanism of exon ligation by human spliceosome.,Zhan X, Lu Y, Zhang X, Yan C, Shi Y Mol Cell. 2022 Aug 4;82(15):2769-2778.e4. doi: 10.1016/j.molcel.2022.05.021. Epub , 2022 Jun 14. PMID:35705093 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures Eukaryotic initiation factor 3D structures Helicase 3D structures Nucleoprotein 3D structures Pre-mRNA splicing factors 3D structures

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