1f1z
From Proteopedia
(New page: 200px<br /><applet load="1f1z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f1z, resolution 2.40Å" /> '''TNSA, a catalytic co...) |
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- | [[Image:1f1z.gif|left|200px]]<br /><applet load="1f1z" size=" | + | [[Image:1f1z.gif|left|200px]]<br /><applet load="1f1z" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f1z, resolution 2.40Å" /> | caption="1f1z, resolution 2.40Å" /> | ||
'''TNSA, a catalytic component of the TN7 transposition system'''<br /> | '''TNSA, a catalytic component of the TN7 transposition system'''<br /> | ||
==Overview== | ==Overview== | ||
- | Transposition requires a coordinated series of DNA breakage and joining | + | 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== | ==About this Structure== | ||
- | 1F1Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1F1Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Craig, N | + | [[Category: Craig, N L.]] |
[[Category: Dyda, F.]] | [[Category: Dyda, F.]] | ||
- | [[Category: Hickman, A | + | [[Category: Hickman, A B.]] |
[[Category: Li, Y.]] | [[Category: Li, Y.]] | ||
- | [[Category: Mathew, S | + | [[Category: Mathew, S V.]] |
- | [[Category: May, E | + | [[Category: May, E W.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: MG]] | [[Category: MG]] | ||
[[Category: restriction endonuclease fold]] | [[Category: restriction endonuclease fold]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:55 2008'' |
Revision as of 10:33, 21 February 2008
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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 with and as ligands. 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 Thu Feb 21 12:33:55 2008