6R9R
Crystal structure of Csx1 in complex with cyclic oligoadenylate cOA4 conformation 2
6R9R の概要
エントリーDOI | 10.2210/pdb6r9r/pdb |
関連するPDBエントリー | 6QZQ 6QZT 6R7B |
EMDBエントリー | 4691 |
分子名称 | circular RNA (5'-R(P*AP*AP*AP*A)-3'), CRISPR-associated (Cas) DxTHG family (3 entities in total) |
機能のキーワード | crispr associated protein carf hepn rnase, rna binding protein |
由来する生物種 | Sulfolobus islandicus REY15A 詳細 |
タンパク質・核酸の鎖数 | 5 |
化学式量合計 | 158383.14 |
構造登録者 | |
主引用文献 | Molina, R.,Stella, S.,Feng, M.,Sofos, N.,Jauniskis, V.,Pozdnyakova, I.,Lopez-Mendez, B.,She, Q.,Montoya, G. Structure of Csx1-cOA4complex reveals the basis of RNA decay in Type III-B CRISPR-Cas. Nat Commun, 10:4302-4302, 2019 Cited by PubMed Abstract: Type III CRISPR-Cas multisubunit complexes cleave ssRNA and ssDNA. These activities promote the generation of cyclic oligoadenylate (cOA), which activates associated CRISPR-Cas RNases from the Csm/Csx families, triggering a massive RNA decay to provide immunity from genetic invaders. Here we present the structure of Sulfolobus islandicus (Sis) Csx1-cOA complex revealing the allosteric activation of its RNase activity. SisCsx1 is a hexamer built by a trimer of dimers. Each dimer forms a cOA binding site and a ssRNA catalytic pocket. cOA undergoes a conformational change upon binding in the second messenger binding site activating ssRNA degradation in the catalytic pockets. Activation is transmitted in an allosteric manner through an intermediate HTH domain, which joins the cOA and catalytic sites. The RNase functions in a sequential cooperative fashion, hydrolyzing phosphodiester bonds in 5'-C-C-3'. The degradation of cOA by Ring nucleases deactivates SisCsx1, suggesting that this enzyme could be employed in biotechnological applications. PubMed: 31541109DOI: 10.1038/s41467-019-12244-z 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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