1lau

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[[Image:1lau.jpg|left|200px]]
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{{STRUCTURE_1lau| PDB=1lau | SCENE= }}
{{STRUCTURE_1lau| PDB=1lau | SCENE= }}
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'''URACIL-DNA GLYCOSYLASE'''
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===URACIL-DNA GLYCOSYLASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 7845459 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7845459}}
==About this Structure==
==About this Structure==
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[[Category: Glycosidase]]
[[Category: Glycosidase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:44:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:09:20 2008''

Revision as of 09:09, 2 July 2008

Image:1lau.png

Template:STRUCTURE 1lau

URACIL-DNA GLYCOSYLASE

Template:ABSTRACT PUBMED 7845459

About this Structure

1LAU is a Single protein structure of sequence from Human herpesvirus 1. 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 Jul 2 12:09:20 2008

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