2F9D

2.5 angstrom resolution structure of the spliceosomal protein p14 bound to region of SF3b155

2F9D の概要

• エントリーDOI: 10.2210/pdb2f9d/pdb
• 分子名称: Pre-mRNA branch site protein p14, Splicing factor 3B subunit 1 (3 entities in total)
• 機能のキーワード: p14 sf3bp14 sf3b155 sap155 rrm, rna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus : Q9Y3B4; Nucleus speckle: O75533
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 39916.83

構造登録者

Schellenberg, M.J.,Edwards, R.A.,Ritchie, D.B.,Glover, J.N.M.,Macmillan, A.M. (登録日: 2005-12-05, 公開日: 2006-01-24, 最終更新日: 2024-10-30)

主引用文献

Schellenberg, M.J.,Edwards, R.A.,Ritchie, D.B.,Kent, O.A.,Golas, M.M.,Stark, H.,Glover, J.N.M.,Macmillan, A.M.
Crystal structure of a core spliceosomal protein interface
Proc.Natl.Acad.Sci.Usa, 103:1266-1271, 2006

PubMed Abstract: The precise excision of introns from precursor mRNAs (pre-mRNAs) in eukaryotes is accomplished by the spliceosome, a complex assembly containing five small nuclear ribonucleoprotein (snRNP) particles. Human p14, a component of the spliceosomal U2 and U11/U12 snRNPs, has been shown to associate directly with the pre-mRNA branch adenosine early in spliceosome assembly and within the fully assembled spliceosome. Here we report the 2.5-A crystal structure of a complex containing p14 and a peptide derived from the p14-associated U2 snRNP component SF3b155. p14 contains an RNA recognition motif (RRM), the surface of which is largely occluded by a C-terminal alpha-helix and a portion of the SF3b155 peptide. An analysis of RNA.protein crosslinking to wild-type and mutant p14 shows that the branch adenosine directly interacts with a conserved aromatic within a pocket on the surface of the complex. This result, combined with a comparison of the structure with known RRMs and pseudoRRMs as well as model-building by using the electron cryomicroscopy structure of a spliceosomal U11/U12 di-snRNP, suggests that p14.SF3b155 presents a noncanonical surface for RNA recognition at the heart of the mammalian spliceosome.

PubMed: 16432215
DOI: 10.1073/pnas.0508048103

実験手法

X-RAY DIFFRACTION (2.5 Å)