› 6ar1

X-ray diffraction
3.01Å resolution

Structure of a Thermostable Group II Intron Reverse Transcriptase with Template-Primer and Its Functional and Evolutionary Implications (RT/Duplex (Nat))

Released:
DOI: 10.2210/pdb6ar1/pdb
PDB entry 6ar1 coloured by chain, front view.
PDB entry 6ar1 coloured by chain, side view.
PDB entry 6ar1 coloured by chain, top view.
Source organisms:
Primary publication:
Structure of a Thermostable Group II Intron Reverse Transcriptase with Template-Primer and Its Functional and Evolutionary Implications.
Stamos JL, Lentzsch AM, Lambowitz AM
Mol Cell 68 926-939.e4 (2017)
PMID: 29153391

Function and Biology Details

Reaction catalysed: 
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
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-119577 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
1 distinct RNA molecule
Macromolecules (3 distinct):
Reverse transcriptase domain-containing protein Chains: A, D
Molecule details ›
Chains: A, D
Length: 428 amino acids
Theoretical weight: 49.81 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: E2GM63 (Residues: 1-420; Coverage: 100%)
Gene name: trt
Sequence domains:
DNA Chains: B, E
Molecule details ›
Chains: B, E
Length: 11 nucleotides
Theoretical weight: 3.3 KDa
Source organism: synthetic construct
Expression system: Not provided
RNA Chains: C, F
Molecule details ›
Chains: C, F
Length: 14 nucleotides
Theoretical weight: 4.46 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand DTP 2 x DTP
Ligand SO4 2 x SO4
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: C2
Unit cell:
a: 179.151Å b: 95.052Å c: 71.567Å
α: 90° β: 113.55° γ: 90°
R-values:
R R work R free
0.218 0.216 0.255
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

Structural Biology of Telomerase.
Wang et al. (2019)
3 more

17 mentions without citation

Structure of Telomerase with Telomeric DNA.
Jiang et al. (2018)
16 more