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2.7.7.B22: transposase

This is an abbreviated version!
For detailed information about transposase, go to the full flat file.

Word Map on EC 2.7.7.B22

Reaction

binds to the ends of a transposon (DNA that moves) and catalyzes the movement of the transposon to another part of the genome by a cut and paste mechanism or a replicative transposition mechanism =

Synonyms

Ac transposase, AcTPase, APM_2825, Buster, DbuzGalileo, DDE-type integrase/transposase/recombinase, DDE_Tnp_1_7 domain-containing protein, DNA transposase, ECO103_3558, Galileo transposase, hAT transposase, hAT-transposase 1, Hermes, Hermes transposase, Hsmar1 transposase, ICE6013, IS10 transposase, IS1341-type transposase, IS1634 transposase, IS200 transposase, IS30-like transposase, IS608, IS711, ISC1041, Kat1, maize activator transposase, mariner transposase, Mbar_A1742, PGM, piggyBac transposase, PiggyMac, Rev 1 transposase, Rev 2 transposase, SB transposase, SB100X, SETMAR, sleeping beauty transposase, SSO1474, Ta0474, Tgf2 TPase, Tgf2 transposase, Tgf2TPase, Tn4430 TnpA, Tn5, Tn5 transposase, Tn7 transposase, TnpA, TnpA 155-amino acid transposase, TnpA transposase, TnsA, TnsB, Tol2, Tpase, transposase for transposon Tn4430, transposase for transposon Tn5, wbk IS transposase, wbkA flanking transposase, wbkA-flanking IS

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.B22 transposase

Crystallization

Crystallization on EC 2.7.7.B22 - transposase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
puriifed recombinant tagged transposase catalytic domain SB100X, residues 114-340, by hanging drop vapour diffusion method, mixing of 0.002 ml of 19 mg/ml protein in 20 mM HEPES, pH 7.2, 50 mM NaCl, 2% v/v glycerol, 10 mM MgCl2, and 0.2 mM TCEP, with 0.002 ml of precipitant solution containing 0.1 M Na-citrate, pH 4.8, and 3.2 M ammonium sulfate, 4°C, 5 days, X-ray diffraction structure determination and analysis at 1.40 A resolution, PDB ID 3HOS
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cocrystal structures of the Hermes transposase bound to DNA that mimics the reaction step immediately prior to hairpin formation. A large DNA conformational change occurs between the initial cleavage step and subsequent hairpin formation that changes which strand is acted upon by a single active site. The complement of divalent metal ions bound by the catalytically essential DDE residues, and the identity of the -2 flanking base pair affect the conformationbal change. For efficient hairpin formation an A:T basepair is favored at the -2 position. The histidine residue within a conserved C/DxxH motif interacts directly with the scissile phosphate
hanging drop vapor diffusion method at 24°C, crystal structure of the enzyme in both Mn2+-bound and Mn2+-free forms
hanging-drop vapour-diffusion method, crystallized at 24°C using a reservoir solution consisting of 100 mM Na HEPES pH 7.5 and 20%(v/v) ethanol. X-ray diffraction data are collected to 1.78 A. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 65.00, b = 34.07, c = 121.58 A, alpha = 90, beta = 100.20, gamma = 90
cryo-EM structures of piggyBac transpososomes show a synaptic complex with hairpin DNA intermediates and a strand transfer complex capturing the integration step. The excised TTAA hairpin intermediate and the TTAA target adopt essentially identical conformations. The transposase forms an asymmetric dimer in which the two central domains synapse the ends while two C-terminal domains form a separate dimer that contacts only one transposon end. In the strand transfer structure, target DNA is severely bent and the TTAA target is unpaired
the C-terminal cysteine-rich domain, PB(552-594), forms a monomeric folded Zn2+-complexed structure