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4R79

Mos1 transposase paired-end complex with left transposon end

Summary for 4R79
Entry DOI10.2210/pdb4r79/pdb
Related2F7T 3HOS 3HOT 4U7B
Descriptorleft Inverted repeat NTS, left Inverted repeat TS, left Inverted repeat NTS H, ... (7 entities in total)
Functional Keywordstransposase, protein-dna complex, transpososome, rnase-h like catalytic fold helix-turn-helix, dna transposition, dna cleavage, dna integration, transposon, inverted repeats, recombination-dna complex, recombination/dna
Biological sourceDrosophila mauritiana (Fruit fly)
More
Cellular locationNucleus : 4R79
Total number of polymer chains8
Total formula weight130662.03
Authors
Richardson, J.M. (deposition date: 2014-08-27, release date: 2015-04-22, Last modification date: 2024-10-16)
Primary citationTrubitsyna, M.,Grey, H.,Houston, D.R.,Finnegan, D.J.,Richardson, J.M.
Structural Basis for the Inverted Repeat Preferences of mariner Transposases.
J.Biol.Chem., 290:13531-13540, 2015
Cited by
PubMed Abstract: The inverted repeat (IR) sequences delimiting the left and right ends of many naturally active mariner DNA transposons are non-identical and have different affinities for their transposase. We have compared the preferences of two active mariner transposases, Mos1 and Mboumar-9, for their imperfect transposon IRs in each step of transposition: DNA binding, DNA cleavage, and DNA strand transfer. A 3.1 Å resolution crystal structure of the Mos1 paired-end complex containing the pre-cleaved left IR sequences reveals the molecular basis for the reduced affinity of the Mos1 transposase DNA-binding domain for the left IR as compared with the right IR. For both Mos1 and Mboumar-9, in vitro DNA transposition is most efficient when the preferred IR sequence is present at both transposon ends. We find that this is due to the higher efficiency of cleavage and strand transfer of the preferred transposon end. We show that the efficiency of Mboumar-9 transposition is improved almost 4-fold by changing the 3' base of the preferred Mboumar-9 IR from guanine to adenine. This preference for adenine at the reactive 3' end for both Mos1 and Mboumar-9 may be a general feature of mariner transposition.
PubMed: 25869132
DOI: 10.1074/jbc.M115.636704
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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