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1udg
From Proteopedia
(New page: 200px<br /><applet load="1udg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1udg, resolution 1.75Å" /> '''THE STRUCTURAL BASIS...) |
Revision as of 13:23, 21 February 2008
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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 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
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