2we1 | pdb_00002we1

EBV DUTPASE MUTANT ASP131ASN WITH BOUND DUMP

spinqualitylabelsall models 2we1, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2we1 is a 1 chain structure with sequence from Ebvb9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4, UMP Related: 2bsy, 2we0, 2we2, 2bt1, 2we3 Activity: dUTP diphosphatase, with EC number 3.6.1.23 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum 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 Deoxyuridine 5'-triphosphate pyrophosphatases (dUTPases) are ubiquitous enzymes essential for hydrolysis of dUTP, thus preventing its incorporation into DNA. Although Epstein-Barr virus (EBV) dUTPase is monomeric, it has a high degree of similarity with the more frequent trimeric form of the enzyme. In both cases, the active site is composed of five conserved sequence motifs. Structural and functional studies of mutants based on the structure of EBV dUTPase gave new insight into the mechanism of the enzyme. A first mutant allowed us to exclude a role in enzymatic activity for the disulfide bridge involving the beginning of the disordered C terminus. Sequence alignments revealed two groups of dUTPases, based on the position in sequence of a conserved aspartic acid residue close to the active site. Single mutants of this residue in EBV dUTPase showed a highly impaired catalytic activity, which could be partially restored by a second mutation, making EBV dUTPase more similar to the second group of enzymes. Deletion of the flexible C-terminal tail carrying motif V resulted in a protein completely devoid of enzymatic activity, crystallizing with unhydrolyzed Mg(2+)-dUTP complex in the active site. Point mutations inside motif V highlighted the essential role of lid residue Phe(273). Magnesium appears to play a role mainly in substrate binding, since in absence of Mg(2+), the K(m) of the enzyme is reduced, whereas the k(cat) is less affected. The flexible motif V of Epstein-Barr virus deoxyuridine 5'-triphosphate pyrophosphatase is essential for catalysis.,Freeman L, Buisson M, Tarbouriech N, Van der Heyden A, Labbe P, Burmeister WP J Biol Chem. 2009 Sep 11;284(37):25280-9. Epub 2009 Jul 7. PMID:19586911 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Deoxyuridine 5'-triphosphate nucleotidohydrolase

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