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- W2195399314 abstract "We present the crystal structure of the junction-resolving enzyme GEN1 bound to DNA at 2.5 Å resolution. The structure of the GEN1 protein reveals it to have an elaborated FEN-XPG family fold that is modified for its role in four-way junction resolution. The functional unit in the crystal is a monomer of active GEN1 bound to the product of resolution cleavage, with an extensive DNA binding interface for both helical arms. Within the crystal lattice, a GEN1 dimer interface juxtaposes two products, whereby they can be reconnected into a four-way junction, the structure of which agrees with that determined in solution. The reconnection requires some opening of the DNA structure at the center, in agreement with permanganate probing and 2-aminopurine fluorescence. The structure shows that a relaxation of the DNA structure accompanies cleavage, suggesting how second-strand cleavage is accelerated to ensure productive resolution of the junction." @default.
- W2195399314 created "2016-06-24" @default.
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- W2195399314 date "2015-12-01" @default.
- W2195399314 modified "2023-10-16" @default.
- W2195399314 title "Crystal Structure of a Eukaryotic GEN1 Resolving Enzyme Bound to DNA" @default.
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- W2195399314 doi "https://doi.org/10.1016/j.celrep.2015.11.042" @default.
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