7abf | pdb_00007abf

Human pre-Bact-1 spliceosome core structure

spinqualitylabelsall models 7abf, resolution 3.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7abf is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.9Å Ligands: GTP, IHP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BUD31_HUMAN Publication Abstract from PubMed Spliceosome activation involves extensive protein and RNA rearrangements that lead to formation of a catalytically active U2/U6 RNA structure. At present, little is known about the assembly pathway of the latter and the mechanism whereby proteins aid its proper folding. Here, we report the cryo-electron microscopy structures of two human, activated spliceosome precursors (that is, pre-B(act) complexes) at core resolutions of 3.9 and 4.2 angstroms. These structures elucidate the order of the numerous protein exchanges that occur during activation, the mutually exclusive interactions that ensure the correct order of ribonucleoprotein rearrangements needed to form the U2/U6 catalytic RNA, and the stepwise folding pathway of the latter. Structural comparisons with mature B(act) complexes reveal the molecular mechanism whereby a conformational change in the scaffold protein PRP8 facilitates final three-dimensional folding of the U2/U6 catalytic RNA. Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation.,Townsend C, Leelaram MN, Agafonov DE, Dybkov O, Will CL, Bertram K, Urlaub H, Kastner B, Stark H, Luhrmann R Science. 2020 Dec 18;370(6523):eabc3753. doi: 10.1126/science.abc3753. Epub 2020 , Nov 26. PMID:33243851 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nucleoprotein 3D structures Pre-mRNA splicing factors 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA