alexa Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans.
Chemical Engineering

Chemical Engineering

Journal of Thermodynamics & Catalysis

Author(s): Leiros I, Moe E, Smals AO, McSweeney S

Abstract Share this page

Abstract Uracil-DNA glycosylases are DNA-repair enzymes that catalyse the removal of promutagenic uracil from single- and double-stranded DNA, thereby initiating the base-excision repair (BER) pathway. Uracil in DNA can occur by mis-incorporation of dUMP in place of dTMP during DNA synthesis or by deamination of cytosine, resulting in U-A or U-G mispairs. The radiation-resistant bacterium Deinococcus radiodurans has an elevated number of uracil-DNA glycosylases compared with most other organisms. The crystal structure of dr0689 (uracil-DNA N-glycosylase), which has been shown to be the major contributor to the removal of mis-incorporated uracil bases in crude cell extracts of D. radiodurans, is reported. This article was published in Acta Crystallogr D Biol Crystallogr and referenced in Journal of Thermodynamics & Catalysis

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

  • Global Conference on Physical Chemistry
    September 18-19, 2017 Dublin, Ireland
  • 2nd International Conference on Applied Chemistry
    October 16-17, 2017 Toronto, Canada
  • 2nd International Conference and Exhibition on Polymer Chemistry
    November 06-08, 2017 Chicago, USA
  • International Conference on Nuclear Chemistry
    December 8-9 , 2016 San Antonio, Texas, USA
Peer Reviewed Journals
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version