4F3E
Crystal Structure of Thermus thermophilus HB8 CasA
4F3E の概要
エントリーDOI | 10.2210/pdb4f3e/pdb |
分子名称 | CasA (2 entities in total) |
機能のキーワード | four helix bundle, cascade complex, immune system |
由来する生物種 | Thermus thermophilus |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 112546.25 |
構造登録者 | |
主引用文献 | Mulepati, S.,Orr, A.,Bailey, S. Crystal Structure of the Largest Subunit of a Bacterial RNA-guided Immune Complex and Its Role in DNA Target Binding. J.Biol.Chem., 287:22445-22449, 2012 Cited by PubMed Abstract: Prokaryotes make use of small RNAs encoded by CRISPR (clustered regularly interspaced short palindromic repeat) loci to provide immunity against bacteriophage or plasmid invasion. In Escherichia coli, the CRISPR-associated complex for antiviral defense (Cascade) utilizes these RNAs to target foreign DNA for destruction. CasA, the largest subunit of Cascade, is essential for its function. Here we report the crystal structure of Thermus thermophilus CasA. The structure is composed of two domains that are arranged in a chair-like conformation with a novel fold forming the larger N-terminal domain. Docking of the crystal structure into cryo-electron microscopy maps reveals two loops in CasA that likely have important functions in DNA target binding. Finally, DNA binding experiments show that CasA is essential for binding of Cascade to DNA target. PubMed: 22621933DOI: 10.1074/jbc.C112.379503 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.4 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード