1lau: Difference between revisions

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<StructureSection load='1lau' size='340' side='right'caption='[[1lau]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1lau' size='340' side='right'caption='[[1lau]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1lau]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1LAU FirstGlance]. <br>
<table><tr><td colspan='2'>[[1lau]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1 Human alphaherpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LAU FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1lau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lau OCA], [http://pdbe.org/1lau PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lau RCSB], [http://www.ebi.ac.uk/pdbsum/1lau PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lau ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lau OCA], [https://pdbe.org/1lau PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lau RCSB], [https://www.ebi.ac.uk/pdbsum/1lau PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lau ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/UNG_HHV11 UNG_HHV11]] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosine. Therefore may reduce deleterious uracil incorporation into the viral genome, particularly, in terminally differentiated neurons which lack DNA repair enzymes.<ref>PMID:7552746</ref> <ref>PMID:16306042</ref>
[https://www.uniprot.org/uniprot/UNG_HHV11 UNG_HHV11] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosine. Therefore may reduce deleterious uracil incorporation into the viral genome, particularly, in terminally differentiated neurons which lack DNA repair enzymes.<ref>PMID:7552746</ref> <ref>PMID:16306042</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lau ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lau ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:7845459</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1lau" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human herpesvirus 1]]
[[Category: Human alphaherpesvirus 1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pearl, L H]]
[[Category: Pearl LH]]
[[Category: Savva, R]]
[[Category: Savva R]]
[[Category: Dna]]
[[Category: Glycosidase]]
[[Category: Hydrolase]]
[[Category: Hydrolase-dna complex]]

Latest revision as of 07:31, 14 February 2024

URACIL-DNA GLYCOSYLASE

1lau, resolution 1.80Å

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