<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f1z ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
Revision as of 02:23, 9 February 2016
TNSA, a catalytic component of the TN7 transposition system
1f1z is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[TNSA_ECOLX] Required for Tn7 transposition. Forms the transposase, together with TnsB. TnsA executes the 5'-DNA strand breakage reaction. TnsABC and TnsD promote high-frequency insertion of Tn7 into a specific target site known as ATT-Tn7 whereas TnsABC and TnsD promote low-frequency insertion into many different sites.[1][2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Sarnovsky RJ, May EW, Craig NL. The Tn7 transposase is a heteromeric complex in which DNA breakage and joining activities are distributed between different gene products. EMBO J. 1996 Nov 15;15(22):6348-61. PMID:8947057
↑Biery MC, Lopata M, Craig NL. A minimal system for Tn7 transposition: the transposon-encoded proteins TnsA and TnsB can execute DNA breakage and joining reactions that generate circularized Tn7 species. J Mol Biol. 2000 Mar 17;297(1):25-37. PMID:10704304 doi:https://dx.doi.org/10.1006/jmbi.2000.3558
↑Hickman AB, Li Y, Mathew SV, May EW, Craig NL, Dyda F. Unexpected structural diversity in DNA recombination: the restriction endonuclease connection. Mol Cell. 2000 Jun;5(6):1025-34. PMID:10911996
