5LSL

Crystal structure of yeast Hsh49p in complex with Cus1p binding domain.

Summary for 5LSL

• Entry DOI: 10.2210/pdb5lsl/pdb
• Related: 5LSB
• Descriptor: Protein HSH49, Cold sensitive U2 snRNA suppressor 1 (3 entities in total)
• Functional Keywords: splicing, u2 snrnp, sf3b complex, rna binding domain
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus : Q99181 Q02554
• Total number of polymer chains: 8
• Total formula weight: 84004.20

Authors

van Roon, A.M.,Obayashi, E.,Sposito, B.,Oubridge, C.,Nagai, K. (deposition date: 2016-09-02, release date: 2017-04-12, Last modification date: 2024-01-17)

Primary citation

van Roon, A.M.,Oubridge, C.,Obayashi, E.,Sposito, B.,Newman, A.J.,Seraphin, B.,Nagai, K.
Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain.
RNA, 23:968-981, 2017

PubMed Abstract: Spliceosomal proteins Hsh49p and Cus1p are components of SF3b, which together with SF3a, Msl1p/Lea1p, Sm proteins, and U2 snRNA, form U2 snRNP, which plays a crucial role in pre-mRNA splicing. Hsh49p, comprising two RRMs, forms a heterodimer with Cus1p. We determined the crystal structures of full-length Hsh49p as well as its RRM1 in complex with a minimal binding region of Cus1p (residues 290-368). The structures show that the Cus1 fragment binds to the α-helical surface of Hsh49p RRM1, opposite the four-stranded β-sheet, leaving the canonical RNA-binding surface available to bind RNA. Hsh49p binds the 5' end region of U2 snRNA via RRM1. Its affinity is increased in complex with Cus1(290-368)p, partly because an extended RNA-binding surface forms across the protein-protein interface. The Hsh49p RRM1-Cus1(290-368)p structure fits well into cryo-EM density of the B spliceosome, corroborating the biological relevance of our crystal structure.

PubMed: 28348170
DOI: 10.1261/rna.059378.116

Experimental method

X-RAY DIFFRACTION (1.65 Å)