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| {{STRUCTURE_2j8x| PDB=2j8x | SCENE= }} | | {{STRUCTURE_2j8x| PDB=2j8x | SCENE= }} |
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| '''EPSTEIN-BARR VIRUS URACIL-DNA GLYCOSYLASE IN COMPLEX WITH UGI FROM PBS-2'''
| | ===EPSTEIN-BARR VIRUS URACIL-DNA GLYCOSYLASE IN COMPLEX WITH UGI FROM PBS-2=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17157317}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17157317 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17157317}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Uracil-dna glycosylase inhibitor]] | | [[Category: Uracil-dna glycosylase inhibitor]] |
| [[Category: Uracil-dna glycosylase,hydrolase]] | | [[Category: Uracil-dna glycosylase,hydrolase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:31:43 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:52:11 2008'' |
