Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
Prokaryotic transposon 5 (Tn5) serves as a model system for studying the molecular mechanism of DNA transposition. Elucidation of the X-ray co-crystal structure of Tn5 transposase complexed with a DNA recognition end sequence provided the first three-dimensional picture of an intermediate in a transposition/retroviral integration pathway. The many Tn5 transposase-DNA co-crystal structures now available complement biochemical and genetic studies, allowing a comprehensive and detailed understanding of transposition mechanisms. Specifically, the structures reveal two different types of protein-DNA contacts: cis contacts, required for initial DNA recognition, and trans contacts, required for catalysis. Protein-protein contacts required for synapsis are also seen. Finally, the two divalent metals in the active site of the transposase support a 'two-metal-ion' mechanism for Tn5 transposition.
Structure/function insights into Tn5 transposition.,Steiniger-White M, Rayment I, Reznikoff WS Curr Opin Struct Biol. 2004 Feb;14(1):50-7. PMID:15102449[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Steiniger-White M, Rayment I, Reznikoff WS. Structure/function insights into Tn5 transposition. Curr Opin Struct Biol. 2004 Feb;14(1):50-7. PMID:15102449 doi:http://dx.doi.org/10.1016/j.sbi.2004.01.008
