2f7t: Difference between revisions
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'''Crystal structure of the catalytic domain of Mos1 mariner transposase''' | {{Structure | ||
|PDB= 2f7t |SIZE=350|CAPTION= <scene name='initialview01'>2f7t</scene>, resolution 2.25Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of the catalytic domain of Mos1 mariner transposase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2F7T is a [ | 2F7T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_mauritiana Drosophila mauritiana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F7T OCA]. | ||
==Reference== | ==Reference== | ||
Mechanism of Mos1 transposition: insights from structural analysis., Richardson JM, Dawson A, O'Hagan N, Taylor P, Finnegan DJ, Walkinshaw MD, EMBO J. 2006 Mar 22;25(6):1324-34. Epub 2006 Mar 2. PMID:[http:// | Mechanism of Mos1 transposition: insights from structural analysis., Richardson JM, Dawson A, O'Hagan N, Taylor P, Finnegan DJ, Walkinshaw MD, EMBO J. 2006 Mar 22;25(6):1324-34. Epub 2006 Mar 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16511570 16511570] | ||
[[Category: Drosophila mauritiana]] | [[Category: Drosophila mauritiana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rnase-h like fold]] | [[Category: rnase-h like 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 16:49:07 2008'' | ||
Revision as of 14:49, 20 March 2008
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| 2f7t, resolution 2.25Å | |||||||||||||
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| Ligands: | MG | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of the catalytic domain of Mos1 mariner transposase
Overview
We present the crystal structure of the catalytic domain of Mos1 transposase, a member of the Tc1/mariner family of transposases. The structure comprises an RNase H-like core, bringing together an aspartic acid triad to form the active site, capped by N- and C-terminal alpha-helices. We have solved structures with either one Mg2+ or two Mn2+ ions in the active site, consistent with a two-metal mechanism for catalysis. The lack of hairpin-stabilizing structural motifs is consistent with the absence of a hairpin intermediate in Mos1 excision. We have built a model for the DNA-binding domain of Mos1 transposase, based on the structure of the bipartite DNA-binding domain of Tc3 transposase. Combining this with the crystal structure of the catalytic domain provides a model for the paired-end complex formed between a dimer of Mos1 transposase and inverted repeat DNA. The implications for the mechanisms of first and second strand cleavage are discussed.
About this Structure
2F7T is a Single protein structure of sequence from Drosophila mauritiana. Full crystallographic information is available from OCA.
Reference
Mechanism of Mos1 transposition: insights from structural analysis., Richardson JM, Dawson A, O'Hagan N, Taylor P, Finnegan DJ, Walkinshaw MD, EMBO J. 2006 Mar 22;25(6):1324-34. Epub 2006 Mar 2. PMID:16511570
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