2DT7

Solution structure of the second SURP domain of human splicing factor SF3a120 in complex with a fragment of human splicing factor SF3a60

Summary for 2DT7

• Entry DOI: 10.2210/pdb2dt7/pdb
• Related: 2DT6
• NMR Information: BMRB: 11365
• Descriptor: Splicing factor 3A subunit 3, Splicing factor 3 subunit 1 (2 entities in total)
• Functional Keywords: structure genomics, sf3a120, sf3a60, surp domain, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, rna binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus speckle: Q12874; Nucleus (By similarity): Q15459
• Total number of polymer chains: 2
• Total formula weight: 14442.38

Authors

He, F.,Kuwasako, K.,Inoue, M.,Guntert, P.,Muto, Y.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2006-07-11, release date: 2006-12-26, Last modification date: 2024-05-29)

Primary citation

Kuwasako, K.,He, F.,Inoue, M.,Tanaka, A.,Sugano, S.,Guentert, P.,Muto, Y.,Yokoyama, S.
Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP
Structure, 14:1677-1689, 2006

PubMed Abstract: The SF3a complex, consisting of SF3a60, SF3a66, and SF3a120, in 17S U2 snRNP is crucial to spliceosomal assembly. SF3a120 contains two tandem SURP domains (SURP1 and SURP2), and SURP2 is responsible for binding to SF3a60. We found that the SURP2 fragment forms a stable complex with an SF3a60 fragment (residues 71-107) and solved its structure by NMR spectroscopy. SURP2 exhibits a fold of the alpha1-alpha2-3(10)-alpha3 topology, and the SF3a60 fragment forms an amphipathic alpha helix intimately contacting alpha1 of SURP2. We also solved the SURP1 structure, which has the same fold as SURP2. The protein-binding interface of SURP2 is quite similar to the corresponding surface of SURP1, except for two amino acid residues. One of them, Leu169, is characteristic of SF3a120 SURP2 among SURP domains. Mutagenesis showed that this single Leu residue is the critical determinant for complex formation, which reveals the protein recognition mechanism in the subunit assembly.

PubMed: 17098193
DOI: 10.1016/j.str.2006.09.009

Experimental method

SOLUTION NMR