1lau

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[[Image:1lau.jpg|left|200px]]
[[Image:1lau.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1lau", creates the "Structure Box" on the page.
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{{STRUCTURE_1lau| PDB=1lau | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lau OCA], [http://www.ebi.ac.uk/pdbsum/1lau PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lau RCSB]</span>
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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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[[Category: dna]]
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[[Category: Dna]]
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[[Category: glycosidase]]
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[[Category: Glycosidase]]
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[[Category: hydrolase]]
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[[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 Sun Mar 30 22:00:29 2008''
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Revision as of 20:44, 2 May 2008

Image:1lau.jpg

Template:STRUCTURE 1lau

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

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