4C97

Cas6 (TTHA0078) H37A mutant

4C97 の概要

• エントリーDOI: 10.2210/pdb4c97/pdb
• 関連するPDBエントリー: 4C8Y 4C8Z 4C98 4C9D
• 分子名称: CAS6A, SULFATE ION (3 entities in total)
• 機能のキーワード: hydrolase, crispr cas protein rna processing ribonuclease
• 由来する生物種: THERMUS THERMOPHILUS HB8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53411.06

構造登録者

Jinek, M.,Niewoehner, O.,Doudna, J.A. (登録日: 2013-10-02, 公開日: 2013-11-06, 最終更新日: 2023-12-20)

主引用文献

Niewoehner, O.,Jinek, M.,Doudna, J.A.
Evolution of Crispr RNA Recognition and Processing by Cas6 Endonucleases.
Nucleic Acids Res., 42:1341-, 2014

PubMed Abstract: In many bacteria and archaea, small RNAs derived from clustered regularly interspaced short palindromic repeats (CRISPRs) associate with CRISPR-associated (Cas) proteins to target foreign DNA for destruction. In Type I and III CRISPR/Cas systems, the Cas6 family of endoribonucleases generates functional CRISPR-derived RNAs by site-specific cleavage of repeat sequences in precursor transcripts. CRISPR repeats differ widely in both sequence and structure, with varying propensity to form hairpin folds immediately preceding the cleavage site. To investigate the evolution of distinct mechanisms for the recognition of diverse CRISPR repeats by Cas6 enzymes, we determined crystal structures of two Thermus thermophilus Cas6 enzymes both alone and bound to substrate and product RNAs. These structures show how the scaffold common to all Cas6 endonucleases has evolved two binding sites with distinct modes of RNA recognition: one specific for a hairpin fold and the other for a single-stranded 5'-terminal segment preceding the hairpin. These findings explain how divergent Cas6 enzymes have emerged to mediate highly selective pre-CRISPR-derived RNA processing across diverse CRISPR systems.

PubMed: 24150936
DOI: 10.1093/NAR/GKT922

実験手法

X-RAY DIFFRACTION (1.7 Å)