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. 2021 Aug 4;596(7871):296–300. doi: 10.1038/s41586-021-03789-5

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — a, Conformation of the SF3B1 and Hsh155 HEAT domains and position of the U2–BS helix and U2 snRNA SLI and SLIIa in human 17S U2 snRNP (Protein DataBank (PDB) (https://www.rcsb.org) accession number 6Y5Q) and in the S. cerevisiae pre-A and A complexes (PDB 6G90). These domains were aligned via Hsh155 heat repeats 19–20, Rse1^BPA and U2 SLIIa. Olive green, SLIIa nucleotides; reddish orange, pre-mRNA branch-site nucleotides; purple, BSL nucleotides that later form the U2–BS helix; yellow, BSL nucleotides forming the extended part of the U2–BS helix; dark green, remaining BSL nucleotides; blue, SLI. b, Fit of Prp5^RecA1 into the pre-A EM density. c, Location of the Prp5 RecA1 and RecA2 domains in the pre-A complex. d, Prp5^RecA1 contacts U2 snRNA nucleotides that connect the U2–BS helix to U2 SLIIa. The positions of Prp5 amino acids (located outside of the SAT motif) that when mutated suppress branch-site mutations are indicated in black.