1udh
From Proteopedia
(New page: 200px<br /><applet load="1udh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1udh, resolution 1.75Å" /> '''THE STRUCTURAL BASIS...) |
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| - | [[Image:1udh.gif|left|200px]]<br /><applet load="1udh" size=" | + | [[Image:1udh.gif|left|200px]]<br /><applet load="1udh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1udh, resolution 1.75Å" /> | caption="1udh, resolution 1.75Å" /> | ||
'''THE STRUCTURAL BASIS OF SPECIFIC BASE EXCISION REPAIR BY URACIL-DNA GLYCOSYLASE'''<br /> | '''THE STRUCTURAL BASIS OF SPECIFIC BASE EXCISION REPAIR BY 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== | ||
| - | 1UDH 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] with SO4 and URA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Uridine_nucleosidase Uridine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3] Full crystallographic information is available from [http:// | + | 1UDH 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] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=URA:'>URA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Uridine_nucleosidase Uridine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Uridine nucleosidase]] | [[Category: Uridine nucleosidase]] | ||
| - | [[Category: Pearl, L | + | [[Category: Pearl, L H.]] |
[[Category: Savva, R.]] | [[Category: Savva, R.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: hydrolase (dna-n-glycosidase)]] | [[Category: hydrolase (dna-n-glycosidase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:17 2008'' |
Revision as of 13:23, 21 February 2008
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THE STRUCTURAL BASIS OF SPECIFIC BASE EXCISION REPAIR BY 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
1UDH is a Single protein structure of sequence from Human herpesvirus 4 with and as ligands. Active as Uridine nucleosidase, with EC number 3.2.2.3 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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