2f7t
From Proteopedia
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| , resolution 2.25Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 02:59:03 2008
