6TEO

Crystal structure of a yeast Snu114-Prp8 complex

Summary for 6TEO

• Entry DOI: 10.2210/pdb6teo/pdb
• Descriptor: Pre-mRNA-splicing factor SNU114, Pre-mRNA-splicing factor 8, SULFATE ION, ... (6 entities in total)
• Functional Keywords: snu114-prp8, gtp, splicing
• Biological source: Saccharomyces cerevisiae S288C; More
• Total number of polymer chains: 4
• Total formula weight: 274833.49

Authors

Ganichkin, O.,Jia, J.,Loll, B.,Absmeier, E.,Wahl, M.C. (deposition date: 2019-11-12, release date: 2020-03-18, Last modification date: 2024-10-16)

Primary citation

Jia, J.,Ganichkin, O.M.,Preussner, M.,Absmeier, E.,Alings, C.,Loll, B.,Heyd, F.,Wahl, M.C.
A Snu114-GTP-Prp8 module forms a relay station for efficient splicing in yeast.
Nucleic Acids Res., 48:4572-4584, 2020

PubMed Abstract: The single G protein of the spliceosome, Snu114, has been proposed to facilitate splicing as a molecular motor or as a regulatory G protein. However, available structures of spliceosomal complexes show Snu114 in the same GTP-bound state, and presently no Snu114 GTPase-regulatory protein is known. We determined a crystal structure of Snu114 with a Snu114-binding region of the Prp8 protein, in which Snu114 again adopts the same GTP-bound conformation seen in spliceosomes. Snu114 and the Snu114-Prp8 complex co-purified with endogenous GTP. Snu114 exhibited weak, intrinsic GTPase activity that was abolished by the Prp8 Snu114-binding region. Exchange of GTP-contacting residues in Snu114, or of Prp8 residues lining the Snu114 GTP-binding pocket, led to temperature-sensitive yeast growth and affected the same set of splicing events in vivo. Consistent with dynamic Snu114-mediated protein interactions during splicing, our results suggest that the Snu114-GTP-Prp8 module serves as a relay station during spliceosome activation and disassembly, but that GTPase activity may be dispensable for splicing.

PubMed: 32196113
DOI: 10.1093/nar/gkaa182

Experimental method

X-RAY DIFFRACTION (3.1 Å)