Results tagged “FEN” from The SIBYLS Beamline


Two related manuscripts appear in the April 15 issue of CELL reporting results endo and exo nucleases important for DNA repair. Both groups of researchers made extensive use of the MX capabilities of the SIBYLS beamline to collect critical crystallographic data. The crystal structures of human flap endonuclease (FEN1) in complex with both substrate and product forms of DNA were reported by Susan Tsutakawa et al. in the following manuscript:

Tsutakawa SE, Classen S, Chapados BR, Arvai A, Finger DL, Guenther G, Tomlinson CG, Thompson P, Sarker AH, Shen B, Cooper PK, Grasby JA, and Tainer JA. “ Human Flap Endonuclease Structures, DNA Double Base Flipping and a Unified Understanding of the FEN1 Superfamily. ” Cell, Volume 145, Issue 2, 198-211, 15 April 2011

Published simultaneously by Jill Orans et al is the crystal structure of human exonuclease 1 in complex with DNA substrate.

Orans J, McSweeney EA, Iyer RR, Hast MA, Hellinga HW, Modrich P, Beese LS. “ Structures of Human Exonuclease 1 DNA Complexes Suggest a Unified Mechanism for Nuclease Family. ” Cell, Volume 145, Issue 2, 212-223, 15 April 2011

Together these two manuscripts present exciting insights into the molecular principles governing diverse endo- and exonucleolytic cleavage specificities of members of the RAD2/FEN superfamily of nucleases, which have critical roles in DNA replication and maintenance.

ALS Ring Status

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