2f7t
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(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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Revision as of 17:29, 29 January 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
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