NMR characterization of the interaction of the endonuclease domain of MutL with divalent metal ions and ATP.

NMR characterization of the interaction of the endonuclease domain of MutL with divalent metal ions and ATP.

MutL is a multi-domain protein comprising an N-terminal ATPase domain (NTD) and C-terminal dimerization domain (CTD), connected with flexible linker regions, that plays a key role in DNA mismatch repair. To expand understanding of the regulation mechanism underlying MutL endonuclease activity, our N...

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Bibliographic Details
Main Authors: Ryota Mizushima, Ju Yaen Kim, Isao Suetake, Hiroaki Tanaka, Tomoyo Takai, Narutoshi Kamiya, Yu Takano, Yuichi Mishima, Shoji Tajima, Yuji Goto, Kenji Fukui, Young-Ho Lee
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4047009?pdf=render

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http://europepmc.org/articles/PMC4047009?pdf=render

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