2bt1: Difference between revisions
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EPSTEIN BARR VIRUS DUTPASE IN COMPLEX WITH A,B-IMINO DUTP
OverviewOverview
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.
About this StructureAbout this Structure
2BT1 is a Single protein structure of sequence from Human herpesvirus 4 with MG and DUP as ligands. Active as dUTP diphosphatase, with EC number 3.6.1.23 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases., Tarbouriech N, Buisson M, Seigneurin JM, Cusack S, Burmeister WP, Structure. 2005 Sep;13(9):1299-310. PMID:16154087
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