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'''TNSA, a catalytic component of the TN7 transposition system''' | '''TNSA, a catalytic component of the TN7 transposition system''' | ||
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[[Category: Mathew, S V.]] | [[Category: Mathew, S V.]] | ||
[[Category: May, E W.]] | [[Category: May, E W.]] | ||
[[Category: | [[Category: Restriction endonuclease fold]] | ||
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Revision as of 12:47, 2 May 2008
TNSA, a catalytic component of the TN7 transposition system
Overview
Transposition requires a coordinated series of DNA breakage and joining reactions. The Tn7 transposase contains two proteins: TnsA, which carries out DNA breakage at the 5' ends of the transposon, and TnsB, which carries out breakage and joining at the 3' ends of the transposon. TnsB is a member of the retroviral integrase superfamily whose hallmark is a conserved DDE motif. We report here the structure of TnsA at 2.4 A resolution. Surprisingly, the TnsA fold is that of a type II restriction endonuclease. Thus, Tn7 transposition involves a collaboration between polypeptides, one containing a DDE motif and one that does not. This result indicates that the range of biological processes that utilize restriction enzyme-like folds also includes DNA transposition.
About this Structure
1F1Z is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Unexpected structural diversity in DNA recombination: the restriction endonuclease connection., Hickman AB, Li Y, Mathew SV, May EW, Craig NL, Dyda F, Mol Cell. 2000 Jun;5(6):1025-34. PMID:10911996 Page seeded by OCA on Fri May 2 15:47:27 2008
