Abstract
The prokaryotic MutM protein is a trifunctional DNA base excision repair enzyme that removes a wide range of oxidatively damaged bases, especially 8-oxoguanine, (N-glycosylase activity) and cleaves both the 3′- and 5′-phosphodiester bonds of the resulting apurinic/apyrimidinic site (AP lyase activity). This enzyme possesses a zinc finger motif (-Cys-X2-Cys-X16-Cys-X2-Cys-) at the C terminus, which forms a β-hairpin loop. The positively charged Arg247 and Arg253 on the β-hairpin loop interact with the phosphate groups to pinch the backbone of the lesion-containing strand. This feature establishes that the zinc finger motif is essential for binding of MutM to DNA as well as its enzymatic activities.
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© 2005 Landes Bioscience/Eurekah.com and Kluwer Academic/Plenum Publishers
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Masui, R., Nakagawa, N., Kuramitsu, S. (2005). MutM: Single C2C2 Zinc Finger-DNA Interaction. In: Iuchi, S., Kuldell, N. (eds) Zinc Finger Proteins. Molecular Biology Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/0-387-27421-9_6
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DOI: https://doi.org/10.1007/0-387-27421-9_6
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-306-48229-8
Online ISBN: 978-0-387-27421-8
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