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4C97

Cas6 (TTHA0078) H37A mutant

Summary for 4C97
Entry DOI10.2210/pdb4c97/pdb
Related4C8Y 4C8Z 4C98 4C9D
DescriptorCAS6A, SULFATE ION (3 entities in total)
Functional Keywordshydrolase, crispr cas protein rna processing ribonuclease
Biological sourceTHERMUS THERMOPHILUS HB8
Total number of polymer chains2
Total formula weight53411.06
Authors
Jinek, M.,Niewoehner, O.,Doudna, J.A. (deposition date: 2013-10-02, release date: 2013-11-06, Last modification date: 2023-12-20)
Primary citationNiewoehner, O.,Jinek, M.,Doudna, J.A.
Evolution of Crispr RNA Recognition and Processing by Cas6 Endonucleases.
Nucleic Acids Res., 42:1341-, 2014
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

239149

數據於2025-07-23公開中

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