1muh
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(New page: 200px<br /> <applet load="1muh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1muh, resolution 2.30Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 06:56, 18 November 2007
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CRYSTAL STRUCTURE OF TN5 TRANSPOSASE COMPLEXED WITH TRANSPOSON END DNA
Overview
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 Structure
1MUH is a Single protein structure of sequence from Escherichia coli with MN and MG as ligands. This structure superseeds 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.
Reference
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 Sun Nov 18 09:03:53 2007
