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| | <StructureSection load='1duc' size='340' side='right'caption='[[1duc]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='1duc' size='340' side='right'caption='[[1duc]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1duc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Eiav Eiav]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DUC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1duc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equine_infectious_anemia_virus Equine infectious anemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DUC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DUD:DEOXYURIDINE-5-DIPHOSPHATE'>DUD</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></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]] 2.05Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/dUTP_diphosphatase dUTP diphosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.23 3.6.1.23] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DUD:DEOXYURIDINE-5-DIPHOSPHATE'>DUD</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</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=1duc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1duc OCA], [https://pdbe.org/1duc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1duc RCSB], [https://www.ebi.ac.uk/pdbsum/1duc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1duc ProSAT]</span></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=1duc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1duc OCA], [https://pdbe.org/1duc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1duc RCSB], [https://www.ebi.ac.uk/pdbsum/1duc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1duc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/POL_EIAV9 POL_EIAV9]] During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase.
| + | [https://www.uniprot.org/uniprot/POL_EIAV9 POL_EIAV9] During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Eiav]] | + | [[Category: Equine infectious anemia virus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: DUTP diphosphatase]]
| + | [[Category: Cedergren-Zeppezauer ES]] |
| - | [[Category: Cedergren-Zeppezauer, E S]] | + | [[Category: Dauter Z]] |
| - | [[Category: Dauter, Z]] | + | [[Category: Nyman PO]] |
| - | [[Category: Nyman, P O]] | + | [[Category: Persson R]] |
| - | [[Category: Persson, R]] | + | [[Category: Rosengren AM]] |
| - | [[Category: Rosengren, A M]] | + | [[Category: Wilson KS]] |
| - | [[Category: Wilson, K S]] | + | |
| - | [[Category: Aspartyl protease]]
| + | |
| - | [[Category: Dutpase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Inhibitor complex]]
| + | |
| - | [[Category: Trimeric enzyme]]
| + | |
| Structural highlights
Function
POL_EIAV9 During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The X-ray structures of dUTPase from equine infectious anaemia virus (EIAV) in unliganded and complexed forms have been determined to 1.9 and 2.0 A resolution, respectively. The structures were solved by molecular replacement using Escherichia coli dUTPase as search model. The exploitation of a relatively novel refinement approach for the initial model, combining maximum likelihood refinement with stereochemically unrestrained updating of the model, proved to be of crucial importance and should be of general relevance.EIAV dUTPase is a homotrimer where each subunit folds into a twisted antiparallel beta-barrel with the N and C-terminal portions interacting with adjacent subunits. The C-terminal 14 and 17 amino acid residues are disordered in the crystal structure of the unliganded and complexed enzyme, respectively. Interactions along the 3-fold axis include a water-containing volume (size 207 A3) which has no contact with bulk solvent. It has earlier been shown that a divalent metal ion is essential for catalysis. For the first time, a putative binding site for such a metal ion, in this case Sr2+, is established. The positions of the inhibitor (the non-hydrolysable substrate analogue dUDP) and the metal ion in the complex are consistent with the location of the active centre established for trimeric dUTPase structures, in which subunit interfaces form three surface clefts lined with evolutionary conserved residues. However, a detailed comparison of the active sites of the EIAV and E. coli enzymes reveals some structural differences. The viral enzyme undergoes a small conformational change in the uracil-binding beta-hairpin structure upon dUDP binding not observed in the other known dUTPase structures.
Crystal structure of dUTPase from equine infectious anaemia virus; active site metal binding in a substrate analogue complex.,Dauter Z, Persson R, Rosengren AM, Nyman PO, Wilson KS, Cedergren-Zeppezauer ES J Mol Biol. 1999 Jan 15;285(2):655-73. PMID:9878436[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dauter Z, Persson R, Rosengren AM, Nyman PO, Wilson KS, Cedergren-Zeppezauer ES. Crystal structure of dUTPase from equine infectious anaemia virus; active site metal binding in a substrate analogue complex. J Mol Biol. 1999 Jan 15;285(2):655-73. PMID:9878436 doi:10.1006/jmbi.1998.2332
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