This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2boo
From Proteopedia
|
THE CRYSTAL STRUCTURE OF URACIL-DNA N-GLYCOSYLASE (UNG) FROM DEINOCOCCUS RADIODURANS.
Overview
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.
About this Structure
2BOO is a Single protein structure of sequence from Deinococcus radiodurans with NO3 as ligand. Active as Uridine nucleosidase, with EC number 3.2.2.3 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans., Leiros I, Moe E, Smalas AO, McSweeney S, Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1049-56. Epub 2005, Jul 20. PMID:16041069
Page seeded by OCA on Mon Nov 5 12:25:35 2007
