› 4dm0

X-ray diffraction
2.5Å resolution

TN5 transposase: 20MER OUTSIDE END 2 MN complex

Released:
DOI: 10.2210/pdb4dm0/pdb
PDB entry 4dm0 coloured by chain, front view.
PDB entry 4dm0 coloured by chain, side view.
PDB entry 4dm0 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Two-metal active site binding of a Tn5 transposase synaptic complex.
Lovell S, Goryshin IY, Reznikoff WR, Rayment I
Nat Struct Biol 9 278-81 (2002)
PMID: 11896402

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-117331 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
Transposase for transposon Tn5 Chain: A
Molecule details ›
Chain: A
Length: 477 amino acids
Theoretical weight: 53.37 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q46731 (Residues: 1-476; Coverage: 100%)
Gene names: tnp, tnpA
Sequence domains:
Structure domains:
DNA TRANSFERRED STRAND Chain: B
Molecule details ›
Chain: B
Length: 21 nucleotides
Theoretical weight: 6.53 KDa
Source organism: Escherichia coli
Expression system: Not provided
DNA NON-TRANSFERRED STRAND Chain: C
Molecule details ›
Chain: C
Length: 20 nucleotides
Theoretical weight: 6.05 KDa
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand MN 3 x MN
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P6522
Unit cell:
a: 112.378Å b: 112.378Å c: 232.783Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.172 0.17 0.203
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

13 review citations

Slicer and the argonautes.
Tolia et al. (2007)
12 more

1 mention without citation

The emerging diversity of transpososome architectures.
Dyda et al. (2012)