2j8x
From Proteopedia
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==Overview== | ==Overview== | ||
| - | 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 ... | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2J8X is a | + | 2J8X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4] and [http://en.wikipedia.org/wiki/Phage_pbs1 Phage pbs1] with URE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J8X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: uracil-dna glycosylase inhibitor]] | [[Category: uracil-dna glycosylase inhibitor]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:30:33 2007'' |
Revision as of 13:25, 5 November 2007
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EPSTEIN-BARR VIRUS URACIL-DNA GLYCOSYLASE IN COMPLEX WITH UGI FROM PBS-2
Overview
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.
About this Structure
2J8X is a Protein complex structure of sequences from Human herpesvirus 4 and Phage pbs1 with URE as ligand. Active as Uridine nucleosidase, with EC number 3.2.2.3 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 5 15:30:33 2007
Categories: Human herpesvirus 4 | Phage pbs1 | Protein complex | Uridine nucleosidase | Buisson, M. | Burmeister, W.P. | Geoui, T. | Tarbouriech, N. | URE | Dna repair | Ebv | Epstein-barr virus | Hydrolase | Hydrolase/inhibitor complex | Lytic protein | Uracil-dna glycosylase | Uracil-dna glycosylase inhibitor
