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PDBsum entry 4zkj

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protein ligands Protein-protein interface(s) links
Unknown function PDB id
4zkj

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
285 a.a.
Ligands
GOL ×6
Waters ×249
PDB id:
4zkj
Name: Unknown function
Title: Crystal structure of crispr-associated protein
Structure: Crispr-associated protein cas1. Chain: a, b. Fragment: unp residues 2-289. Engineered: yes
Source: Streptococcus pyogenes m1 476. Organism_taxid: 1207470. Gene: cas1, m1gas476_0831. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.25Å     R-factor:   0.183     R-free:   0.211
Authors: D.Ka,E.Bae
Key ref: D.Ka et al. (2016). Crystal Structure of Streptococcus pyogenes Cas1 and Its Interaction with Csn2 in the Type II CRISPR-Cas System. Structure, 24, 70-79. PubMed id: 26671707 DOI: 10.1016/j.str.2015.10.019
Date:
30-Apr-15     Release date:   13-Jan-16    
PROCHECK
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 Headers
 References

Protein chains
J7M1H5  (J7M1H5_STRP1) - 
Key:    Secondary structure

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

 

 
DOI no: 10.1016/j.str.2015.10.019 Structure 24:70-79 (2016)
PubMed id: 26671707  
 
 
Crystal Structure of Streptococcus pyogenes Cas1 and Its Interaction with Csn2 in the Type II CRISPR-Cas System.
D.Ka, H.Lee, Y.D.Jung, K.Kim, C.Seok, N.Suh, E.Bae.
 
  ABSTRACT  
 
CRISPRs and Cas proteins constitute an RNA-guided microbial immune system against invading nucleic acids. Cas1 is a universal Cas protein found in all three types of CRISPR-Cas systems, and its role is implicated in new spacer acquisition during CRISPR-mediated adaptive immunity. Here, we report the crystal structure of Streptococcus pyogenes Cas1 (SpCas1) in a type II CRISPR-Cas system and characterize its interaction with S. pyogenes Csn2 (SpCsn2). The SpCas1 structure reveals a unique conformational state distinct from type I Cas1 structures, resulting in a more extensive dimerization interface, a more globular overall structure, and a disruption of potential metal-binding sites for catalysis. We demonstrate that SpCas1 directly interacts with SpCsn2, and identify the binding interface and key residues for Cas complex formation. These results provide structural information for a type II Cas1 protein, and lay a foundation for studying multiprotein Cas complexes functioning in type II CRISPR-Cas systems.
 

 

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