1lau
From Proteopedia
(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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| - | [[Image:1lau.jpg|left|200px]]<br /><applet load="1lau" size=" | + | [[Image:1lau.jpg|left|200px]]<br /><applet load="1lau" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lau, resolution 1.800Å" /> | caption="1lau, resolution 1.800Å" /> | ||
'''URACIL-DNA GLYCOSYLASE'''<br /> | '''URACIL-DNA GLYCOSYLASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 1.75-A crystal structure of the uracil-DNA glycosylase from herpes | + | 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== | ==About this Structure== | ||
| - | 1LAU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http:// | + | 1LAU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Pearl, L | + | [[Category: Pearl, L H.]] |
[[Category: Savva, R.]] | [[Category: Savva, R.]] | ||
[[Category: dna]] | [[Category: dna]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:12 2008'' |
Revision as of 11:43, 21 February 2008
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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 Thu Feb 21 13:43:12 2008
