First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
|3cvs, resolution 2.40Å ()|
|Gene:||alkA, aidA (Escherichia coli)|
|Related:||3cvt, 3cw7, 3cwa, 3cws, 3cwt, 3cwu|
Crystal Structure of an AlkA Host/Guest Complex 8oxoGuanine:Adenine Base Pair
The constant attack on DNA by endogenous and exogenous agents gives rise to nucleobase modifications that cause mutations, which can lead to cancer. Visualizing the effects of these lesions on the structure of duplex DNA is key to understanding their biologic consequences. The most definitive method of obtaining such structures, X-ray crystallography, is troublesome to employ owing to the difficulty of obtaining diffraction-quality crystals of DNA. Here, we present a crystallization system that uses a protein, the DNA glycosylase AlkA, as a scaffold to mediate the crystallization of lesion-containing duplex DNA. We demonstrate the use of this system to facilitate the rapid structure determination of DNA containing the lesion 8-oxoguanine in several different sequence contexts, and also deoxyinosine and 1,N(6)-ethenoadenine, each stabilized as the corresponding 2'-flouro analog. The structures of 8-oxoguanine provide a correct atomic-level view of this important endogenous lesion in DNA.
Structure of the E. coli DNA glycosylase AlkA bound to the ends of duplex DNA: a system for the structure determination of lesion-containing DNA., Bowman BR, Lee S, Wang S, Verdine GL, Structure. 2008 Aug 6;16(8):1166-74. PMID:18682218
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Bowman BR, Lee S, Wang S, Verdine GL. Structure of the E. coli DNA glycosylase AlkA bound to the ends of duplex DNA: a system for the structure determination of lesion-containing DNA. Structure. 2008 Aug 6;16(8):1166-74. PMID:18682218 doi:10.1016/j.str.2008.04.012
- Shah N, Kuntz DA, Rose DR. Golgi alpha-mannosidase II cleaves two sugars sequentially in the same catalytic site. Proc Natl Acad Sci U S A. 2008 Jul 15;105(28):9570-5. Epub 2008 Jul 3. PMID:18599462