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4ILM

CRISPR RNA Processing endoribonuclease

Summary for 4ILM
Entry DOI10.2210/pdb4ilm/pdb
Related3PKM 4ILL 4ILR
DescriptorCRISPR-associated endoribonuclease Cas6 2, RNA (5'-R(*GP*CP*UP*AP*AP*UP*CP*UP*AP*CP*UP*AP*UP*AP*GP*A)-3') (2 entities in total)
Functional Keywordsrrm, endoribonuclease, rna, hydrolase-rna complex, hydrolase/rna
Biological sourceSulfolobus solfataricus
More
Total number of polymer chains16
Total formula weight302009.65
Authors
Shao, Y.,Li, H. (deposition date: 2012-12-31, release date: 2013-03-20, Last modification date: 2024-02-28)
Primary citationShao, Y.,Li, H.
Recognition and cleavage of a nonstructured CRISPR RNA by its processing endoribonuclease Cas6.
Structure, 21:385-393, 2013
Cited by
PubMed Abstract: Clustered regularly interspaced short palindromic repeats (CRISPRs) confer adaptive immunity to prokaryotes through a small RNA-mediated mechanism. Specific endoribonucleases are required by all CRISPR-bearing organisms to process CRISPR RNAs into small RNA that serve as guides for defensive effector complexes. The molecular mechanism of how the endoribonucleases process the class of CRISPR RNA containing no predicted secondary structural features remains largely elusive. Here, we report cocrystal structures of a processing endoribonuclease bound with a noncleavable RNA substrate and its product-like fragment derived from a nonpalindramic repeat. The enzyme stabilizes a short RNA stem-loop structure near the cleavage site and cleaves the phosphodiester bond using an active site comprised of arginine and lysine residues. The distinct RNA binding and cleavage mechanisms underline the diversity in CRISPR RNA processing.
PubMed: 23454186
DOI: 10.1016/j.str.2013.01.010
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.068 Å)
Structure validation

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