2f7t

Crystal structure of the catalytic domain of Mos1 mariner transposase

spinqualitylabelsall models 2f7t, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2f7t is a 1 chain structure with sequence from Drosophila mauritiana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transposase

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