4EMH
Crystal structure of SpLsm4
4EMH の概要
エントリーDOI | 10.2210/pdb4emh/pdb |
関連するPDBエントリー | 4EMG 4EMK |
分子名称 | Probable U6 snRNA-associated Sm-like protein LSm4 (2 entities in total) |
機能のキーワード | sm fold, mrna decay, pre-mrna splicing, lsm proteins, rna binding protein |
由来する生物種 | Schizosaccharomyces pombe (Fission yeast) |
細胞内の位置 | Nucleus (Potential): O14352 |
タンパク質・核酸の鎖数 | 24 |
化学式量合計 | 297897.60 |
構造登録者 | |
主引用文献 | Wu, D.H.,Jiang, S.M.,Bowler, M.W.,Song, H.W. Crystal Structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces pombe. Plos One, 7:e36768-e36768, 2012 Cited by PubMed Abstract: Sm-like (Lsm) proteins are ubiquitous and function in many aspects of RNA metabolism, including pre-mRNA splicing, nuclear RNA processing, mRNA decay and miRNA biogenesis. Here three crystal structures including Lsm3, Lsm4 and Lsm5/6/7 sub-complex from S. pombe are reported. These structures show that all the five individual Lsm subunits share a conserved Sm fold, and Lsm3, Lsm4, and Lsm5/6/7 form a heptamer, a trimer and a hexamer within the crystal lattice, respectively. Analytical ultracentrifugation indicates that Lsm3 and Lsm5/6/7 sub-complex exist in solution as a heptamer and a hexamer, respectively while Lsm4 undergoes a dynamic equilibrium between monomer and trimer in solution. RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7. PubMed: 22615807DOI: 10.1371/journal.pone.0036768 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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