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PDBsum entry 4ill

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protein dna_rna Protein-protein interface(s) links
Hydrolase/RNA PDB id
4ill

 

 

 

 

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Contents
Protein chains
278 a.a.
DNA/RNA
Waters ×12
PDB id:
4ill
Name: Hydrolase/RNA
Title: Recognition and cleavage of a non-structured crispr RNA by its processing endoribonuclease cas6
Structure: Crispr-associated endoribonuclease cas6 2. Chain: a, b. Engineered: yes. RNA (5'- r( Gp Cp Up Ap Ap Up Cp Up Ap Cp Up Ap Up Ap Gp Ap Ap Up Up Gp Ap Ap Ap G)-3'). Chain: r, c. Engineered: yes
Source: Sulfolobus solfataricus. Organism_taxid: 273057. Strain: p2. Gene: cas6b, sso2004. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.48Å     R-factor:   0.207     R-free:   0.239
Authors: Y.Shao,H.Li
Key ref: Y.Shao and H.Li (2013). Recognition and cleavage of a nonstructured CRISPR RNA by its processing endoribonuclease Cas6. Structure, 21, 385-393. PubMed id: 23454186 DOI: 10.1016/j.str.2013.01.010
Date:
31-Dec-12     Release date:   20-Mar-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q97WV8  (CAS6B_SULSO) -  CRISPR-associated endoribonuclease Cas6 2 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Seq:
Struc:
289 a.a.
278 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

DNA/RNA chains
  A-A-U-C-U-A-C-U-A-U-A-G-A-A-U-G-A-A-G 19 bases
  G-C-U-A-A-U-C-U-A-C-U-A-U-A-G-A-A 17 bases

 Enzyme reactions 
   Enzyme class: E.C.3.1.-.-
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/j.str.2013.01.010 Structure 21:385-393 (2013)
PubMed id: 23454186  
 
 
Recognition and cleavage of a nonstructured CRISPR RNA by its processing endoribonuclease Cas6.
Y.Shao, H.Li.
 
  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.
 

 

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