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1f1z

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[[Image:1f1z.gif|left|200px]]
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{{STRUCTURE_1f1z| PDB=1f1z | SCENE= }}
{{STRUCTURE_1f1z| PDB=1f1z | SCENE= }}
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'''TNSA, a catalytic component of the TN7 transposition system'''
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===TNSA, a catalytic component of the TN7 transposition system===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10911996 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10911996}}
==About this Structure==
==About this Structure==
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[[Category: May, E W.]]
[[Category: May, E W.]]
[[Category: Restriction endonuclease fold]]
[[Category: Restriction endonuclease fold]]
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Revision as of 23:21, 30 June 2008

Image:1f1z.png

Template:STRUCTURE 1f1z

TNSA, a catalytic component of the TN7 transposition system

Template:ABSTRACT PUBMED 10911996

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 Tue Jul 1 02:21:12 2008

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