1muh
CRYSTAL STRUCTURE OF TN5 TRANSPOSASE COMPLEXED WITH TRANSPOSON END DNA
OverviewOverview
Genomic evolution has been profoundly influenced by DNA transposition, a process whereby defined DNA segments move freely about the genome. Transposition is mediated by transposases, and similar events are catalyzed by retroviral integrases such as human immunodeficiency virus-1 (HIV-1) integrase. Understanding how these proteins interact with DNA is central to understanding the molecular basis of transposition. We report the three-dimensional structure of prokaryotic Tn5 transposase complexed with Tn5 transposon end DNA determined to 2.3 angstrom resolution. The molecular assembly is dimeric, where each double-stranded DNA molecule is bound by both protein subunits, orienting the transposon ends into the active sites. This structure provides a molecular framework for understanding many aspects of transposition, including the binding of transposon end DNA by one subunit and cleavage by a second, cleavage of two strands of DNA by a single active site via a hairpin intermediate, and strand transfer into target DNA.
About this StructureAbout this Structure
1MUH is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1f3i. The following page contains interesting information on the relation of 1MUH with [Transposase]. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of the Tn5 synaptic complex transposition intermediate., Davies DR, Goryshin IY, Reznikoff WS, Rayment I, Science. 2000 Jul 7;289(5476):77-85. PMID:10884228 Page seeded by OCA on Sat May 3 01:43:59 2008