2oxm
From Proteopedia
|
Crystal structure of a UNG2/modified DNA complex that represent a stabilized short-lived extrahelical state in ezymatic DNA base flipping
Overview
The enzyme uracil DNA glycosylase (UNG) excises unwanted uracil bases in, the genome using an extrahelical base recognition mechanism. Efficient, removal of uracil is essential for prevention of C-to-T transition, mutations arising from cytosine deamination, cytotoxic U*A pairs arising, from incorporation of dUTP in DNA, and for increasing immunoglobulin gene, diversity during the acquired immune response. A central event in all of, these UNG-mediated processes is the singling out of rare U*A or U*G base, pairs in a background of approximately 10(9) T*A or C*G base pairs in the, human genome. Here we establish for the human and Escherichia coli enzymes, that discrimination of thymine and uracil is initiated by thermally, induced opening of T*A and U*A base pairs and not by active participation, of the enzyme. Thus, base-pair dynamics has a critical role in the, genome-wide search for uracil, and may be involved in initial damage, recognition by other DNA repair glycosylases.
About this Structure
2OXM is a Protein complex structure of sequences from Homo sapiens. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Enzymatic capture of an extrahelical thymine in the search for uracil in DNA., Parker JB, Bianchet MA, Krosky DJ, Friedman JI, Amzel LM, Stivers JT, Nature. 2007 Sep 27;449(7161):433-7. Epub 2007 Aug 19. PMID:17704764
Page seeded by OCA on Wed Jan 23 12:36:48 2008
