The DNA glycosylase AlkD uses a non-base-flipping mechanism to excise bulky lesions

Elwood A. Mullins, Rongxin Shi, Zachary D. Parsons, Philip K. Yuen, Sheila S. David, Yasuhiro Igarashi and Brandt F. Eichman ()
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Elwood A. Mullins: Vanderbilt University
Rongxin Shi: Vanderbilt University
Zachary D. Parsons: Vanderbilt University
Philip K. Yuen: University of California, Davis
Sheila S. David: University of California, Davis
Yasuhiro Igarashi: Biotechnology Research Center, Toyama Prefectural University
Brandt F. Eichman: Vanderbilt University

Nature, 2015, vol. 527, issue 7577, 254-258

Abstract: Crystal structures of the DNA glycosylase AlkD with DNA containing various modified bases show that neither substrate recognition nor catalysis use a base-flipping mechanism; instead, AlkD scans the phosphodeoxyribose backbone for increased cationic charge imparted by the alkylated base, and then uses the positive charge to facilitate cleavage of the glycosidic bond, thus explaining the specificity of AlkD for cationic lesions.

Date: 2015
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DOI: 10.1038/nature15728

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