› 4c8y

X-ray diffraction
1.8Å resolution

Cas6 (TTHA0078) substrate mimic complex

Released:
DOI: 10.2210/pdb4c8y/pdb
PDB entry 4c8y coloured by chain, front view.
PDB entry 4c8y coloured by chain, side view.
PDB entry 4c8y coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Evolution of CRISPR RNA recognition and processing by Cas6 endonucleases.
Niewoehner O, Jinek M, Doudna JA
Nucleic Acids Res 42 1341-53 (2014)
PMID: 24150936

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178250 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
CRISPR-associated protein Cas6 C-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 243 amino acids
Theoretical weight: 26.58 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SM65 (Residues: 1-239; Coverage: 100%)
Gene name: TTHA0078
Sequence domains: CRISPR-associated endoribonuclease Cas6
Structure domains:
R1 REPEAT RNA SUBSTRATE MIMIC Chain: C
Molecule details ›
Chain: C
Length: 16 nucleotides
Theoretical weight: 5.16 KDa
Source organism: Thermus thermophilus HB8
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P21
Unit cell:
a: 43.07Å b: 83.3Å c: 73.44Å
α: 90° β: 101.41° γ: 90°
R-values:
R R work R free
0.192 0.191 0.216
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

15 review citations

Unravelling the structural and mechanistic basis of CRISPR-Cas systems.
van der Oost et al. (2014)
14 more

3 mentions without citation

Not making the cut: Techniques to prevent RNA cleavage in structural studies of RNase-RNA complexes.
Jones et al. (2022)
2 more