2BT1

Epstein Barr Virus dUTPase in complex with a,b-imino dUTP

Summary for 2BT1

• Entry DOI: 10.2210/pdb2bt1/pdb
• Related: 2BSY
• Descriptor: DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE, 2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: dutpase, monomer, hydrolase, nucleotide metabolism, structural proteomics in europe, spine, structural genomics
• Biological source: HUMAN HERPESVIRUS 4 (EPSTEIN-BARR VIRUS)
• Total number of polymer chains: 1
• Total formula weight: 31486.00

Authors

Tarbouriech, N.,Buisson, M.,Seigneurin, J.-M.,Cusack, S.,Burmeister, W.P. (deposition date: 2005-05-24, release date: 2005-09-15, Last modification date: 2024-11-20)

Primary citation

Tarbouriech, N.,Buisson, M.,Seigneurin, J.-M.,Cusack, S.,Burmeister, W.P.
The Monomeric Dutpase from Epstein-Barr Virus Mimics Trimeric Dutpases
Structure, 13:1299-, 2005

PubMed Abstract: Deoxyuridine 5'-triphosphate pyrophosphatases (dUTPases) are ubiquitous enzymes cleaving dUTP into dUMP and pyrophosphate. They occur as monomeric, dimeric, or trimeric molecules. The trimeric and monomeric enzymes both contain the same five characteristic sequence motifs but in a different order, whereas the dimeric enzymes are not homologous. Monomeric dUTPases only occur in herpesviruses, such as Epstein-Barr virus (EBV). Here, we describe the crystal structures of EBV dUTPase in complex with the product dUMP and a substrate analog alpha,beta-imino-dUTP. The molecule consists of three domains forming one active site that has a structure extremely similar to one of the three active sites of trimeric dUTPases. The three domains functionally correspond to the subunits of the trimeric form. Domains I and II have the dUTPase fold, but they differ considerably in the regions that are not involved in the formation of the unique active site, whereas domain III has only little secondary structure.

PubMed: 16154087
DOI: 10.1016/J.STR.2005.06.009

Experimental method

X-RAY DIFFRACTION (2.7 Å)