1udh: Difference between revisions

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{{STRUCTURE_1udh|  PDB=1udh  |  SCENE=  }}  
{{STRUCTURE_1udh|  PDB=1udh  |  SCENE=  }}  


'''THE STRUCTURAL BASIS OF SPECIFIC BASE EXCISION REPAIR BY URACIL-DNA GLYCOSYLASE'''
===THE STRUCTURAL BASIS OF SPECIFIC BASE EXCISION REPAIR BY URACIL-DNA GLYCOSYLASE===




==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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{{ABSTRACT_PUBMED_7845459}}


==About this Structure==
==About this Structure==
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[[Category: Pearl, L H.]]
[[Category: Pearl, L H.]]
[[Category: Savva, R.]]
[[Category: Savva, R.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:04:13 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:48:51 2008''

Revision as of 20:48, 28 July 2008

File:1udh.png

Template:STRUCTURE 1udh

THE STRUCTURAL BASIS OF SPECIFIC BASE EXCISION REPAIR BY URACIL-DNA GLYCOSYLASE

Template:ABSTRACT PUBMED 7845459

About this Structure

1UDH 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

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