Journal
CELL REPORTS
Volume 13, Issue 11, Pages 2565-2575Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2015.11.042
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Funding
- Cancer Research UK
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council [BB/E001777/1] Funding Source: researchfish
- Cancer Research UK [11722] Funding Source: researchfish
- BBSRC [BB/E001777/1] Funding Source: UKRI
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We present the crystal structure of the junction-resolving enzyme GEN1 bound to DNA at 2.5 angstrom 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.
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