1lau
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(New page: 200px<br /><applet load="1lau" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lau, resolution 1.800Å" /> '''URACIL-DNA GLYCOSYL...)
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Revision as of 18:18, 20 November 2007
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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
1LAU is a Single protein structure of sequence from Human herpesvirus 4. 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 Tue Nov 20 20:26:04 2007
