2VJV: Crystal Structure Of The Is608 Transposase In Complex With Left End 26-Mer Dna Hairpin And A 6-Mer Dna Representing The Left End Cleavage Site

The smallest known DNA transposases are those from the IS200/IS605 family. Here we show how the interplay of protein and DNA activates TnpA, the Helicobacter pylori IS608 transposase, for catalysis. First, transposon end binding causes a conformational change that aligns catalytically important protein residues within the active site. Subsequent precise cleavage at the left and right ends, the steps that liberate the transposon from its donor site, does not involve a site-specific DNA-binding domain. Rather, cleavage site recognition occurs by complementary base pairing with a TnpA-bound subterminal transposon DNA segment. Thus, the enzyme active site is constructed from elements of both protein and DNA, reminiscent of the interdependence of protein and RNA in the ribosome. Our structural results explain why the transposon ends are asymmetric and how the transposon selects a target site for integration, and they allow us to propose a molecular model for the entire transposition reaction.
PDB ID: 2VJVDownload
MMDB ID: 62535
PDB Deposition Date: 2007/12/13
Updated in MMDB: 2011/10
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 2VJV: hexameric; determined by author and by software (PQS)
Molecular Components in 2VJV
Label Count Molecule
Proteins (2 molecules)
Transposase Orfa
Molecule annotation
Nucleotides(2 molecules)
5'-d(*da*da*da*dg*dc*dc*dc*dc*dt*da*dg*dc*dtp*dt *dt*dt*da*dg*dc*dt*da*dt*dg*dg*dg*dgp)-3'
Molecule annotation
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB