2BOO
The crystal structure of Uracil-DNA N-Glycosylase (UNG) from Deinococcus radiodurans.
Summary for 2BOO
| Entry DOI | 10.2210/pdb2boo/pdb |
| Descriptor | URACIL-DNA GLYCOSYLASE, NITRATE ION (3 entities in total) |
| Functional Keywords | base excision repair, radiation resistance, dna damage, dna repair, glycosidase, hydrolase |
| Biological source | DEINOCOCCUS RADIODURANS |
| Total number of polymer chains | 1 |
| Total formula weight | 27966.51 |
| Authors | Leiros, I.,Moe, E.,Smalas, A.O.,McSweeney, S. (deposition date: 2005-04-13, release date: 2005-07-27, Last modification date: 2023-12-13) |
| Primary citation | Leiros, I.,Moe, E.,Smalas, A.O.,Mcsweeney, S. Structure of the Uracil-DNA N-Glycosylase (Ung) from Deinococcus Radiodurans. Acta Crystallogr.,Sect.D, 61:1049-, 2005 Cited by PubMed 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. PubMed: 16041069DOI: 10.1107/S090744490501382X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
