› 3kyl

X-ray diffraction
2.7Å resolution

Structure of the catalytic subunit of telomerase bound to its RNA template and telomeric DNA

Released:
DOI: 10.2210/pdb3kyl/pdb
PDB entry 3kyl coloured by chain, front view.
PDB entry 3kyl coloured by chain, side view.
PDB entry 3kyl coloured by chain, top view.
Source organism: Tribolium castaneum
Primary publication:
Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA.
Mitchell M, Gillis A, Futahashi M, Fujiwara H, Skordalakes E
Nat Struct Mol Biol 17 513-8 (2010)
PMID: 20357774

Function and Biology Details

Reaction catalysed: 
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-113131 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA/RNA hybrid molecule
Macromolecules (2 distinct):
Telomerase reverse transcriptase Chain: A
Molecule details ›
Chain: A
Length: 596 amino acids
Theoretical weight: 70.59 KDa
Source organism: Tribolium castaneum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0QHL8 (Residues: 1-596; Coverage: 100%)
Gene names: AUGUSTUS-3.0.2_10963, TERT, TcasGA2_TC010963
Sequence domains:
Structure domains:
DNA/RNA (5'-R(*CP*UP*GP*AP*CP*CP*UP*GP*AP*C)-D(P*TP*TP*CP*GP*GP*TP*CP*AP*GP*GP*TP*CP*AP*G)-3') Chain: E
Molecule details ›
Chain: E
Length: 24 nucleotides
Theoretical weight: 7.49 KDa
Source organism: Tribolium castaneum
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 77.231Å b: 52.782Å c: 101.609Å
α: 90° β: 101.9° γ: 90°
R-values:
R R work R free
0.245 0.242 0.287
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

29 review citations

Biogenesis of telomerase ribonucleoproteins.
Egan et al. (2012)
28 more

44 mentions without citation

Finding the end: recruitment of telomerase to telomeres.
Nandakumar et al. (2013)
43 more