2OYT

Crystal Structure of UNG2/DNA(TM)

Summary for 2OYT

• Entry DOI: 10.2210/pdb2oyt/pdb
• Related: 2OXM
• Descriptor: Uracil-DNA glycosylase, DNA strand1, DNA strand2, ... (4 entities in total)
• Functional Keywords: enzyme-dna complex, ung2, hydrolase-dna complex, hydrolase/dna
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Mitochondrion. Isoform 2: Nucleus: P13051
• Total number of polymer chains: 3
• Total formula weight: 31213.95

Authors

Bianchet, M.A.,Krosky, D.J.,Stivers, J.T.,Amzel, L.M. (deposition date: 2007-02-22, release date: 2007-10-30, Last modification date: 2023-08-30)

Primary citation

Parker, J.B.,Bianchet, M.A.,Krosky, D.J.,Friedman, J.I.,Amzel, L.M.,Stivers, J.T.
Enzymatic capture of an extrahelical thymine in the search for uracil in DNA.
Nature, 449:433-437, 2007

PubMed Abstract: 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.

PubMed: 17704764
DOI: 10.1038/nature06131

Experimental method

X-RAY DIFFRACTION (2 Å)