Structure/function insights into Tn5 transposition.
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.
Steiniger-White
Mindy
M
University of Wisconsin-Madison, Department of Biochemistry, 433 Babcock Drive, Madison, WI 53706, USA. mmsteini@wisc.edu
Rayment
Ivan
I
Reznikoff
William S
WS
D002384:Catalysis; D004247:DNA / Q000378:metabolism*; D004251:DNA Transposable Elements / Q000235:genetics*; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D019895:Transposases / Q000737:chemistry / Q000378:metabolism*
D004251:DNA Transposable Elements; C473503:Tn5 transposase; D004247:DNA; D019895:Transposases