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1lau
From Proteopedia
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[[Image:1lau.jpg|left|200px]] | [[Image:1lau.jpg|left|200px]] | ||
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'''URACIL-DNA GLYCOSYLASE''' | '''URACIL-DNA GLYCOSYLASE''' | ||
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[[Category: Pearl, L H.]] | [[Category: Pearl, L H.]] | ||
[[Category: Savva, R.]] | [[Category: Savva, R.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:44:00 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:44, 2 May 2008
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 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 Fri May 2 23:44:00 2008
