1f1z: Difference between revisions
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[[Image:1f1z.gif|left|200px]] | [[Image:1f1z.gif|left|200px]] | ||
'''TNSA, a catalytic component of the TN7 transposition system''' | {{Structure | ||
|PDB= 1f1z |SIZE=350|CAPTION= <scene name='initialview01'>1f1z</scene>, resolution 2.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''TNSA, a catalytic component of the TN7 transposition system''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1F1Z is a [ | 1F1Z is a [[Single protein]] structure of 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]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10911996 10911996] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: restriction endonuclease fold]] | [[Category: restriction endonuclease fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:17 2008'' | ||
Revision as of 09:03, 20 March 2008
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| 1f1z, resolution 2.40Å | |||||||||||||
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| Ligands: | MG and CL | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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