8DO6
The structure of S. epidermidis Cas10-Csm bound to target RNA
8DO6 の概要
エントリーDOI | 10.2210/pdb8do6/pdb |
EMDBエントリー | 27593 |
分子名称 | CRISPR system Cms endoribonuclease Csm3, crRNA, Target RNA, ... (6 entities in total) |
機能のキーワード | crispr, cas10, type iii, csm, rna binding protein, rna binding protein-rna complex, rna binding protein/rna |
由来する生物種 | Staphylococcus epidermidis RP62A 詳細 |
タンパク質・核酸の鎖数 | 9 |
化学式量合計 | 205217.08 |
構造登録者 | |
主引用文献 | Paraan, M.,Nasef, M.,Chou-Zheng, L.,Khweis, S.A.,Schoeffler, A.J.,Hatoum-Aslan, A.,Stagg, S.M.,Dunkle, J.A. The structure of a Type III-A CRISPR-Cas effector complex reveals conserved and idiosyncratic contacts to target RNA and crRNA among Type III-A systems. Plos One, 18:e0287461-e0287461, 2023 Cited by PubMed Abstract: Type III CRISPR-Cas systems employ multiprotein effector complexes bound to small CRISPR RNAs (crRNAs) to detect foreign RNA transcripts and elicit a complex immune response that leads to the destruction of invading RNA and DNA. Type III systems are among the most widespread in nature, and emerging interest in harnessing these systems for biotechnology applications highlights the need for detailed structural analyses of representatives from diverse organisms. We performed cryo-EM reconstructions of the Type III-A Cas10-Csm effector complex from S. epidermidis bound to an intact, cognate target RNA and identified two oligomeric states, a 276 kDa complex and a 318 kDa complex. 3.1 Å density for the well-ordered 276 kDa complex allowed construction of atomic models for the Csm2, Csm3, Csm4 and Csm5 subunits within the complex along with the crRNA and target RNA. We also collected small-angle X-ray scattering data which was consistent with the 276 kDa Cas10-Csm architecture we identified. Detailed comparisons between the S. epidermidis Cas10-Csm structure and the well-resolved bacterial (S. thermophilus) and archaeal (T. onnurineus) Cas10-Csm structures reveal differences in how the complexes interact with target RNA and crRNA which are likely to have functional ramifications. These structural comparisons shed light on the unique features of Type III-A systems from diverse organisms and will assist in improving biotechnologies derived from Type III-A effector complexes. PubMed: 37352230DOI: 10.1371/journal.pone.0287461 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.1 Å) |
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