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Literature summary for 2.7.7.B22 extracted from

  • Morellet, N.; Li, X.; Wieninger, S.A.; Taylor, J.L.; Bischerour, J.; Moriau, S.; Lescop, E.; Bardiaux, B.; Mathy, N.; Assrir, N.; Betermier, M.; Nilges, M.; Hickman, A.B.; Dyda, F.; Craig, N.L.; Guittet, E.
    Sequence-specific DNA binding activity of the cross-brace zinc finger motif of the piggyBac transposase (2018), Nucleic Acids Res., 46, 2660-2677 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.B22

Crystallization (Commentary)

Crystallization (Comment) Organism
the C-terminal cysteine-rich domain, PB(552-594), forms a monomeric folded Zn2+-complexed structure Trichoplusia ni

Protein Variants

Protein Variants Comment Organism
K569A mutant exhibits a sharp decrease in its apparent binding affinity to LE1-35 substrate Trichoplusia ni
R567A mutant exhibits a sharp decrease in its apparent binding affinity to LE1-35 substrate Trichoplusia ni
Y558A mutant exhibits a decrease in its apparent binding affinity to LE1-35 substrate Trichoplusia ni

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ the C-terminal cysteine-rich domain, PB(552-594), forms a monomeric folded Zn2+-complexed structure. 2D NMR spectroscopy of the domain, residues C559, C562, C582 and H585 on the one hand, and C574, C577, C590 and C593 on the other hand are oriented to coordinate two Zn2+ Trichoplusia ni

Organism

Organism UniProt Comment Textmining
Trichoplusia ni Q27026
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Synonyms

Synonyms Comment Organism
DDE_Tnp_1_7 domain-containing protein
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 Trichoplusia ni
piggyBac transposase
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 Trichoplusia ni

General Information

General Information Comment Organism
physiological function the C-terminal cysteine-rich domain is essential for DNA breakage, joining and transposition. The region of amino acids 530-594 binds to specific DNA sequences in the left and right transposon ends, and to an additional internal site at the left end. The C-terminal cysteine-rich domain adopts the specific fold of the cross-brace zinc finger protein family and interacts with the 5'-TGCGT-3'/3'-ACGCA-5' motif of the 19-bp repeats Trichoplusia ni