2f7t
From Proteopedia
(New page: 200px<br /><applet load="2f7t" size="350" color="white" frame="true" align="right" spinBox="true" caption="2f7t, resolution 2.25Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | We present the crystal structure of the catalytic domain of Mos1 | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dawson, A.]] | [[Category: Dawson, A.]] | ||
| - | [[Category: Finnegan, D | + | [[Category: Finnegan, D J.]] |
| - | [[Category: Richardson, J | + | [[Category: Richardson, J M.]] |
[[Category: Taylor, P.]] | [[Category: Taylor, P.]] | ||
| - | [[Category: Walkinshaw, M | + | [[Category: Walkinshaw, M D.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: ddd motif]] | [[Category: ddd motif]] | ||
[[Category: rnase-h like fold]] | [[Category: rnase-h like fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:18:38 2008'' |
Revision as of 15:18, 21 February 2008
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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 with as ligand. 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
Page seeded by OCA on Thu Feb 21 17:18:38 2008
