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From Proteopedia
Crystal structure of the Mos1 mariner paired end complex with Mn
Structural highlights
FunctionMOS1T_DROMA Mediates transposition of transposon Mos1 by a 'cut and paste' mechanism. Transposases are sequence-specific nucleases and strand transferases that catalyze transposition through an ordered series of events: sequence-specific binding of transposase to the terminal inverted repeats (IR) present at each end of the transposon, pairing of the transposon IRs in a paired-end complex (PEC), cleavage of one or both DNA strands at each transposon end, capture of target DNA, and strand transfer to insert the transposon at a new site. 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 PubMedA key step in cut-and-paste DNA transposition is the pairing of transposon ends before the element is excised and inserted at a new site in its host genome. Crystallographic analyses of the paired-end complex (PEC) formed from precleaved transposon ends and the transposase of the eukaryotic element Mos1 reveals two parallel ends bound to a dimeric enzyme. The complex has a trans arrangement, with each transposon end recognized by the DNA binding region of one transposase monomer and by the active site of the other monomer. Two additional DNA duplexes in the crystal indicate likely binding sites for flanking DNA. Biochemical data provide support for a model of the target capture complex and identify Arg186 to be critical for target binding. Mixing experiments indicate that a transposase dimer initiates first-strand cleavage and suggest a pathway for PEC formation. Molecular architecture of the Mos1 paired-end complex: the structural basis of DNA transposition in a eukaryote.,Richardson JM, Colloms SD, Finnegan DJ, Walkinshaw MD Cell. 2009 Sep 18;138(6):1096-108. PMID:19766564[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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