Iron-catalysed oxidation intermediates captured in a DNA repair dioxygenase
Chengqi Yi,
Guifang Jia,
Guanhua Hou,
Qing Dai,
Wen Zhang,
Guanqun Zheng,
Xing Jian,
Cai-Guang Yang,
Qiang Cui and
Chuan He ()
Additional contact information
Chengqi Yi: The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA
Guifang Jia: The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA
Guanhua Hou: University of Wisconsin, 1101 University Avenue
Qing Dai: The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA
Wen Zhang: The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA
Guanqun Zheng: The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA
Xing Jian: The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA
Cai-Guang Yang: The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA
Qiang Cui: University of Wisconsin, 1101 University Avenue
Chuan He: The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA
Nature, 2010, vol. 468, issue 7321, 330-333
Abstract:
Oxidation intermediates in a DNA repair dioxygenase The AlkB type proteins are demethylases that are thought to play a part in DNA repair by oxidatively removing methyl adducts on DNA, RNA and histones. Yi et al. have determined the structure of AlkB oxygenase crystallized in complex with various modified DNAs. By growing the crystals under anaerobic conditions and then exposing them to dioxygen to initiate oxidation, two different intermediates were trapped. A third type of intermediate was determined using additional computational analysis. These structures provide detailed mechanistic insight into how these enzymes perform oxidative demethylation.
Date: 2010
References: Add references at CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/nature09497 Abstract (text/html)
Access to the full text of the articles in this series is restricted.
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:468:y:2010:i:7321:d:10.1038_nature09497
Ordering information: This journal article can be ordered from
https://www.nature.com/
DOI: 10.1038/nature09497
Access Statistics for this article
Nature is currently edited by Magdalena Skipper
More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().