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PDBsum entry 4cmq

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4cmq
Jmol PyMol
Contents
Protein chains
1156 a.a.
Ligands
SO4 ×6
Metals
_MN ×13
PDB id:
4cmq
Name: Hydrolase
Title: Crystal structure of mn-bound s.Pyogenes cas9
Structure: Crispr-associated endonuclease cas9/csn1. Chain: a, b. Synonym: cas9. Engineered: yes
Source: Streptococcus pyogenes. Organism_taxid: 301447. Strain: serotype m1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta 2.
Resolution:
3.09Å     R-factor:   0.250     R-free:   0.277
Authors: M.Jinek,F.Jiang,D.W.Taylor,S.H.Sternberg,E.Kaya,E.Ma,C.Ander M.Hauer,K.Zhou,S.Lin,M.Kaplan,A.T.Iavarone,E.Charpentier,E. J.A.Doudna
Key ref: M.Jinek et al. (2014). Structures of Cas9 endonucleases reveal RNA-mediated conformational activation. Science, 343, 1247997. PubMed id: 24505130 DOI: 10.1126/science.1247997
Date:
17-Jan-14     Release date:   12-Feb-14    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q99ZW2  (Q99ZW2_STRP1) -  CRISPR-associated endonuclease Cas9/Csn1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1368 a.a.
1156 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.3.1.-.-
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     nucleic acid phosphodiester bond hydrolysis   3 terms 
  Biochemical function     hydrolase activity     9 terms  

 

 
DOI no: 10.1126/science.1247997 Science 343:1247997 (2014)
PubMed id: 24505130  
 
 
Structures of Cas9 endonucleases reveal RNA-mediated conformational activation.
M.Jinek, F.Jiang, D.W.Taylor, S.H.Sternberg, E.Kaya, E.Ma, C.Anders, M.Hauer, K.Zhou, S.Lin, M.Kaplan, A.T.Iavarone, E.Charpentier, E.Nogales, J.A.Doudna.
 
  ABSTRACT  
 
Type II CRISPR (clustered regularly interspaced short palindromic repeats)-Cas (CRISPR-associated) systems use an RNA-guided DNA endonuclease, Cas9, to generate double-strand breaks in invasive DNA during an adaptive bacterial immune response. Cas9 has been harnessed as a powerful tool for genome editing and gene regulation in many eukaryotic organisms. We report 2.6 and 2.2 angstrom resolution crystal structures of two major Cas9 enzyme subtypes, revealing the structural core shared by all Cas9 family members. The architectures of Cas9 enzymes define nucleic acid binding clefts, and single-particle electron microscopy reconstructions show that the two structural lobes harboring these clefts undergo guide RNA-induced reorientation to form a central channel where DNA substrates are bound. The observation that extensive structural rearrangements occur before target DNA duplex binding implicates guide RNA loading as a key step in Cas9 activation.
 

 

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