3eug
From Proteopedia
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CRYSTAL STRUCTURE OF ESCHERICHIA COLI URACIL DNA GLYCOSYLASE AND ITS COMPLEXES WITH URACIL AND GLYCEROL: STRUCTURE AND GLYCOSYLASE MECHANISM REVISITED
Overview
The DNA repair enzyme uracil DNA glycosylase (UDG) catalyzes the, hydrolysis of premutagenic uracil residues from single-stranded or duplex, DNA, producing free uracil and abasic DNA. Here we report the, high-resolution crystal structures of free UDG from Escherichia coli, strain B (1.60 A), its complex with uracil (1.50 A), and a second, active-site complex with glycerol (1.43 A). These represent the first, high-resolution structures of a prokaryotic UDG to be reported. The, overall structure of the E. coli enzyme is more similar to the human UDG, than the herpes virus enzyme. Significant differences between the, bacterial and viral structures are seen in the side-chain positions of the, putative general-acid (His187) and base (Asp64), similar to differences, previously observed between ... [(full description)]
About this Structure
3EUG is a [Single protein] structure of sequence from [Escherichia coli] with GOL as [ligand]. Active as [[1]], with EC number [3.2.2.3]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited., Xiao G, Tordova M, Jagadeesh J, Drohat AC, Stivers JT, Gilliland GL, Proteins. 1999 Apr 1;35(1):13-24. PMID:10090282
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