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1f1z

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Revision as of 10:21, 16 October 2019

TNSA, a catalytic component of the TN7 transposition system

Structural highlights

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.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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:http://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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1f1z"

@@ Line 1: / Line 1: @@
 ==TNSA, a catalytic component of the TN7 transposition system==
-<StructureSection load='1f1z' size='340' side='right' caption='[[1f1z]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='1f1z' size='340' side='right'caption='[[1f1z]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1f1z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F1Z FirstGlance]. <br>
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Escherichia coli]]
+[[Category: Large Structures]]
 [[Category: Craig, N L]]
 [[Category: Dyda, F]]

1f1z

From Proteopedia

Revision as of 10:21, 16 October 2019

TNSA, a catalytic component of the TN7 transposition system

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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