› 7qxs

Electron Microscopy
3.9Å resolution

Cryo-EM structure of human telomerase-DNA-TPP1-POT1 complex (with POT1 side chains)

Released:
DOI: 10.2210/pdb7qxs/pdb
PDB entry 7qxs coloured by chain, front view.
PDB entry 7qxs coloured by chain, side view.
PDB entry 7qxs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of human telomerase recruitment by TPP1-POT1.
Sekne Z, Ghanim GE, van Roon AM, Nguyen THD
Science 375 1173-1176 (2022)
PMID: 35201900
Related structures: EMD-14197

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 heptamer (preferred)
PDBe Complex ID:
PDB-CPX-289210 (preferred)
Entry contents:
5 distinct polypeptide molecules
1 distinct DNA molecule
1 distinct RNA molecule
Macromolecules (7 distinct):
Telomerase reverse transcriptase Chain: A
Molecule details ›
Chain: A
Length: 1132 amino acids
Theoretical weight: 127.2 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: O14746 (Residues: 1-1132; Coverage: 100%)
Gene names: EST2, TCS1, TERT, TRT
Sequence domains:
Histone H2A Chain: L
Molecule details ›
Chain: L
Length: 130 amino acids
Theoretical weight: 14.14 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: B2R5B3 (Residues: 1-130; Coverage: 100%)
Sequence domains:
Histone H2B Chain: M
Adrenocortical dysplasia protein homolog Chain: O
Protection of telomeres protein 1 Chain: P
Telomeric DNA Chain: N
RNA (256-MER) Chain: B

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 3.9Å
Relevant EMDB volumes: EMD-14197
Expression systems:
  • Homo sapiens
  • Spodoptera

Quick links

Citations

14 review citations

Genetics of human telomere biology disorders.
Revy et al. (2023)
13 more

5 mentions without citation

Orchestrating nucleic acid-protein interactions at chromosome ends: telomerase mechanisms come into focus.
Lue et al. (2023)
4 more