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What is Lig E? 


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Lig E is a type of DNA ligase that differs from the general paradigm by not requiring complete encirclement of the DNA substrate for engagement. It has been shown that Lig E proteins do not need additional domains or loops for substrate binding, as confirmed by the structure of a Lig E-type DNA ligase bound to the nicked DNA-adenylate reaction intermediate. On the other hand, Lig v 1, a major allergen from privet pollen grains, forms a homodimer and belongs to the Ole e 1 protein family, which promotes specific IgE production leading to allergies through cross-reactivity with other pollen sources. Lig v 1's structure reveals a β-barrel fold stabilized by conserved disulphide bonds, with unique loop structures and a C-terminal α-helix.

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Lig v 1 is a major allergen from the Oleaceae family, specifically from privet pollen grains, known to induce specific IgE production and potentially influence the development of allergies.
Lig E refers to the fused-ring bulky 1,1,3,3,5,5,7,7-octaethyl-s-hydrindacen-4-yl group used in (E)-1,2-diaryldigermenes synthesis, influencing their structural characteristics and absorption properties.
Lig E is a newly identified subunit of RNA polymerase found in Gram-positive bacteria, resembling phage proteins like Gp2, possibly involved in protection from phage infection.
L.E.G.O. is an interactive graphics system for creating, viewing, and manipulating geometric figures and objects, serving as an electronic tool for geometric constructions in teaching geometry and computer graphics.
Lig E is a minimal scaffold DNA ligase that binds DNA without additional domains or loops, demonstrating robust substrate engagement and essential attributes of DNA ligation.

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