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ScharerDavid Orlando

Scharer, Orlando D.
Schärer Lab.
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Crystal structure of a thwarted mismatch glycosylase DNA repair complex

Author(s)
Barrett, Tracey E.Scharer, Orlando D.Savva, RenosBrown, TomJiricny, JosefVerdine, Gregory L.Pearl, Laurence H.
Issued Date
1999-12
DOI
10.1093/emboj/18.23.6599
URI
https://scholarworks.unist.ac.kr/handle/201301/21295
Fulltext
http://emboj.embopress.org/content/18/23/6599
Citation
EMBO JOURNAL, v.18, no.23, pp.6599 - 6609
Abstract
The bacterial mismatch-specific uracil-DNA glycosylase (MUG) and eukaryotic thymine-DNA glycosylase (TDG) enzymes form a homologous family of DNA glycosylases that initiate base-excision repair of G:U/T mismatches. Despite low sequence homology, the MUG/TDG enzymes are structurally related to the uracil-DNA glycosylase enzymes, but have a very different mechanism for substrate recognition. We have now determined the crystal structure of the Escherichia coli R-IUG enzyme complexed with an oligonucleotide containing a non-hydrolysable deoxyuridine analogue mismatched with guanine, providing the first structure of an intact substrate-nucleotide productively bound to a hydrolytic DNA glycosylase. The structure of this complex explains the preference for G:U over G:T mispairs, and reveals an essentially non-specific pyrimidine-binding pocket that allows MUG/TDG enzymes to excise the alkylated base, 3,N(4)-ethenocytosine, Together with structures for the free enzyme and for an abasic-DNA product complex, the MUG-substrate analogue complex reveals the conformational changes accompanying the catalytic cycle of substrate binding, base excision and product release.
Publisher
WILEY-BLACKWELL
ISSN
0261-4189

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