2bt1: Difference between revisions

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-[[Image:2bt1.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2bt1", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_2bt1|  PDB=2bt1  |  SCENE=  }}
-'''EPSTEIN BARR VIRUS DUTPASE IN COMPLEX WITH A,B-IMINO DUTP'''
+==Epstein Barr Virus dUTPase in complex with a,b-imino dUTP==
+<StructureSection load='2bt1' size='340' side='right'caption='[[2bt1]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2bt1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_4 Human gammaherpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BT1 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DUP:2-DEOXYURIDINE+5-ALPHA,BETA-IMIDO-TRIPHOSPHATE'>DUP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2bt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bt1 OCA], [https://pdbe.org/2bt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bt1 RCSB], [https://www.ebi.ac.uk/pdbsum/2bt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bt1 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DUT_EBVB9 DUT_EBVB9] Involved in nucleotide metabolism: produces dUMP, the immediate precursor of thymidine nucleotides and decreases the intracellular concentration of dUTP to avoid uracil incorporation into DNA. Induces immune dysregulation that contributes to the pathophysiology of the virus infection.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bt/2bt1_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2bt1 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Deoxyuridine 5'-triphosphate pyrophosphatases (dUTPases) are ubiquitous enzymes cleaving dUTP into dUMP and pyrophosphate. They occur as monomeric, dimeric, or trimeric molecules. The trimeric and monomeric enzymes both contain the same five characteristic sequence motifs but in a different order, whereas the dimeric enzymes are not homologous. Monomeric dUTPases only occur in herpesviruses, such as Epstein-Barr virus (EBV). Here, we describe the crystal structures of EBV dUTPase in complex with the product dUMP and a substrate analog alpha,beta-imino-dUTP. The molecule consists of three domains forming one active site that has a structure extremely similar to one of the three active sites of trimeric dUTPases. The three domains functionally correspond to the subunits of the trimeric form. Domains I and II have the dUTPase fold, but they differ considerably in the regions that are not involved in the formation of the unique active site, whereas domain III has only little secondary structure.
-==Overview==
+The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases.,Tarbouriech N, Buisson M, Seigneurin JM, Cusack S, Burmeister WP Structure. 2005 Sep;13(9):1299-310. PMID:16154087<ref>PMID:16154087</ref>
-Deoxyuridine 5'-triphosphate pyrophosphatases (dUTPases) are ubiquitous enzymes cleaving dUTP into dUMP and pyrophosphate. They occur as monomeric, dimeric, or trimeric molecules. The trimeric and monomeric enzymes both contain the same five characteristic sequence motifs but in a different order, whereas the dimeric enzymes are not homologous. Monomeric dUTPases only occur in herpesviruses, such as Epstein-Barr virus (EBV). Here, we describe the crystal structures of EBV dUTPase in complex with the product dUMP and a substrate analog alpha,beta-imino-dUTP. The molecule consists of three domains forming one active site that has a structure extremely similar to one of the three active sites of trimeric dUTPases. The three domains functionally correspond to the subunits of the trimeric form. Domains I and II have the dUTPase fold, but they differ considerably in the regions that are not involved in the formation of the unique active site, whereas domain III has only little secondary structure.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-BT1 is a [[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=2BT1 OCA].
+</div>
+<div class="pdbe-citations 2bt1" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases., Tarbouriech N, Buisson M, Seigneurin JM, Cusack S, Burmeister WP, Structure. 2005 Sep;13(9):1299-310. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16154087 16154087]
+*[[DUTPase 3D structures|DUTPase 3D structures]]
-[[Category: Human herpesvirus 4]]
+== References ==
-[[Category: Single protein]]
+<references/>
-[[Category: DUTP diphosphatase]]
+__TOC__
-[[Category: Buisson, M.]]
+</StructureSection>
-[[Category: Burmeister, W P.]]
+[[Category: Human gammaherpesvirus 4]]
-[[Category: Cusack, S.]]
+[[Category: Large Structures]]
-[[Category: SPINE, Structural Proteomics in Europe.]]
+[[Category: Buisson M]]
-[[Category: Seigneurin, J M.]]
+[[Category: Burmeister WP]]
-[[Category: Tarbouriech, N.]]
+[[Category: Cusack S]]
-[[Category: Dutpase]]
+[[Category: Seigneurin J-M]]
-[[Category: Hydrolase]]
+[[Category: Tarbouriech N]]
-[[Category: Monomer]]
-[[Category: Nucleotide metabolism]]
-[[Category: Spine]]
-[[Category: Structural genomic]]
-[[Category: Structural proteomics in europe]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:18:29 2008''