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| | <StructureSection load='2j8x' size='340' side='right'caption='[[2j8x]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2j8x' size='340' side='right'caption='[[2j8x]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2j8x]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bppb2 Bppb2] and [http://en.wikipedia.org/wiki/Ebvg Ebvg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J8X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J8X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2j8x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bppb2 Bppb2] and [https://en.wikipedia.org/wiki/Ebvg Ebvg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J8X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=URE:UREA'>URE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=URE:UREA'>URE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eui|1eui]], [[1lqg|1lqg]], [[1lqm|1lqm]], [[1udi|1udi]], [[1ugh|1ugh]], [[1ugi|1ugi]], [[1uug|1uug]], [[2ugi|2ugi]], [[2uug|2uug]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eui|1eui]], [[1lqg|1lqg]], [[1lqm|1lqm]], [[1udi|1udi]], [[1ugh|1ugh]], [[1ugi|1ugi]], [[1uug|1uug]], [[2ugi|2ugi]], [[2uug|2uug]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Uridine_nucleosidase Uridine nucleosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8x OCA], [http://pdbe.org/2j8x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j8x RCSB], [http://www.ebi.ac.uk/pdbsum/2j8x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8x 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=2j8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8x OCA], [https://pdbe.org/2j8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j8x RCSB], [https://www.ebi.ac.uk/pdbsum/2j8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/UNGI_BPPB2 UNGI_BPPB2]] This protein binds specifically and reversibly to the host uracil-DNA glycosylase, preventing removal of uracil residues from PBS2 DNA by the host uracil-excision repair system. | + | [[https://www.uniprot.org/uniprot/UNGI_BPPB2 UNGI_BPPB2]] This protein binds specifically and reversibly to the host uracil-DNA glycosylase, preventing removal of uracil residues from PBS2 DNA by the host uracil-excision repair system. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[DNA glycosylase|DNA glycosylase]] | + | *[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]] |
| | *[[Uracil glycosylase inhibitor|Uracil glycosylase inhibitor]] | | *[[Uracil glycosylase inhibitor|Uracil glycosylase inhibitor]] |
| | == References == | | == References == |
| Structural highlights
Function
[UNGI_BPPB2] This protein binds specifically and reversibly to the host uracil-DNA glycosylase, preventing removal of uracil residues from PBS2 DNA by the host uracil-excision repair system.
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
Epstein-Barr virus (EBV) is a human gamma-herpesvirus. Within its 86 open reading frame containing genome, two enzymes avoiding uracil incorporation into DNA can be found: uracil triphosphate hydrolase and uracil-DNA glycosylase (UNG). The latter one excises uracil bases that are due to cytosine deamination or uracil misincorporation from double-stranded DNA substrates. The EBV enzyme belongs to family 1 UNGs. We solved the three-dimensional structure of EBV UNG in complex with the uracil-DNA glycosylase inhibitor protein (Ugi) from bacteriophage PBS-2 at a resolution of 2.3 A by X-ray crystallography. The structure of EBV UNG encoded by the BKRF3 reading frame shows the excellent global structural conservation within the solved examples of family 1 enzymes. Four out of the five catalytic motifs are completely conserved, whereas the fifth one, the leucine loop, carries a seven residue insertion. Despite this insertion, catalytic constants of EBV UNG are similar to those of other UNGs. Modelling of the EBV UNG-DNA complex shows that the longer leucine loop still contacts DNA and is likely to fulfil its role of DNA binding and deformation differently than the enzymes with previously solved structures. We could show that despite the evolutionary distance of EBV UNG from the natural host protein, bacteriophage Ugi binds with an inhibitory constant of 8 nM to UNG. This is due to an excellent specificity of Ugi for conserved elements of UNG, four of them corresponding to catalytic motifs and a fifth one corresponding to an important beta-turn structuring the catalytic site.
New insights on the role of the gamma-herpesvirus uracil-DNA glycosylase leucine loop revealed by the structure of the Epstein-Barr virus enzyme in complex with an inhibitor protein.,Geoui T, Buisson M, Tarbouriech N, Burmeister WP J Mol Biol. 2007 Feb 9;366(1):117-31. Epub 2006 Nov 7. PMID:17157317[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Geoui T, Buisson M, Tarbouriech N, Burmeister WP. New insights on the role of the gamma-herpesvirus uracil-DNA glycosylase leucine loop revealed by the structure of the Epstein-Barr virus enzyme in complex with an inhibitor protein. J Mol Biol. 2007 Feb 9;366(1):117-31. Epub 2006 Nov 7. PMID:17157317 doi:10.1016/j.jmb.2006.11.007
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