5EWR
C merolae U4 snRNP protein Snu13
5EWR の概要
| エントリーDOI | 10.2210/pdb5ewr/pdb |
| 分子名称 | Box C/D snoRNP and U4 snRNP component Snu13p (2 entities in total) |
| 機能のキーワード | splicing, rna binding protein |
| 由来する生物種 | Cyanidioschyzon merolae (Red alga) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 15790.30 |
| 構造登録者 | Garside, E.L.,Black, C.,Rader, S.,MacMillan, A.M. (登録日: 2015-11-20, 公開日: 2016-04-20, 最終更新日: 2023-09-27) |
| 主引用文献 | Black, C.S.,Garside, E.L.,MacMillan, A.M.,Rader, S.D. Conserved structure of Snu13 from the highly reduced spliceosome of Cyanidioschyzon merolae. Protein Sci., 25:911-916, 2016 Cited by PubMed Abstract: Structural and functional analysis of proteins involved in pre-mRNA splicing is challenging because of the complexity of the splicing machinery, known as the spliceosome. Bioinformatic, proteomic, and biochemical analyses have identified a minimal spliceosome in the red alga Cyanidioschyzon merolae. This spliceosome consists of only 40 core proteins, compared to ∼ 70 in S. cerevisiae (yeast) and ∼ 150 in humans. We report the X-ray crystallographic analysis of C. merolae Snu13 (CmSnu13), a key component of the assembling spliceosome, and present evidence for conservation of Snu13 function in this algal splicing pathway. The near identity of CmSnu13's three-dimensional structure to yeast and human Snu13 suggests that C. merolae should be an excellent model system for investigating the structure and function of the conserved core of the spliceosome. PubMed: 26833716DOI: 10.1002/pro.2894 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.35 Å) |
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