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Title 

Covalent binding of uracil DNA glycosylase UdgX to abasic DNA upon uracil excision

Authors 

Woo-Chan AhnS AroliJ H KimJeong Hee MoonGa Seal LeeMin-Ho LeeP B SangB H OhU VarshneyEui-Jeon Woo

Publisher 

Nature Publishing Group

Issue Date 

2019

Citation 

Nature Chemical Biology

Abstract 

Uracil DNA glycosylases (UDGs) are important DNA repair enzymes that excise uracil from DNA, yielding an abasic site. Recently, UdgX, an unconventional UDG with extremely tight binding to DNA containing uracil, was discovered. The structure of UdgX from Mycobacterium smegmatis in complex with DNA shows an overall similarity to that of family 4 UDGs except for a protruding loop at the entrance of the uracil-binding pocket. Surprisingly, H109 in the loop was found to make a covalent bond to the abasic site to form a stable intermediate, while the excised uracil remained in the pocket of the active site. H109 functions as a nucleophile to attack the oxocarbenium ion, substituting for the catalytic water molecule found in other UDGs. To our knowledge, this change from a catalytic water attack to a direct nucleophilic attack by the histidine residue is unprecedented. UdgX utilizes a unique mechanism of protecting cytotoxic abasic sites from exposure to the cellular environment.

URI 

https://doi.org/10.1038/s41589-019-0289-3.

ISSN 

1552-4450

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-07-10


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