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.
1udg
From Proteopedia
|
THE STRUCTURAL BASIS OF SPECIFIC BASE EXCISION REPAIR BY URACIL-DNA GLYCOSYLASE
Overview
The 1.75-A crystal structure of the uracil-DNA glycosylase from herpes, simplex virus type-1 reveals a new fold, distantly related to, dinucleotide-binding proteins. Complexes with a trideoxynucleotide, and, with uracil, define the DNA-binding site and allow a detailed, understanding of the exquisitely specific recognition of uracil in DNA., The overall structure suggests binding models for elongated single- and, double-stranded DNA substrates. Conserved residues close to the, uracil-binding site suggest a catalytic mechanism for hydrolytic base, excision.
About this Structure
1UDG is a Single protein structure of sequence from Human herpesvirus 4 with SO4 as ligand. Active as Uridine nucleosidase, with EC number 3.2.2.3 Full crystallographic information is available from OCA.
Reference
The structural basis of specific base-excision repair by uracil-DNA glycosylase., Savva R, McAuley-Hecht K, Brown T, Pearl L, Nature. 1995 Feb 9;373(6514):487-93. PMID:7845459
Page seeded by OCA on Wed Nov 21 04:02:28 2007
