2BT1

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

2BT1 の概要

• エントリーDOI: 10.2210/pdb2bt1/pdb
• 関連するPDBエントリー: 2BSY
• 分子名称: DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE, 2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: dutpase, monomer, hydrolase, nucleotide metabolism, structural proteomics in europe, spine, structural genomics
• 由来する生物種: HUMAN HERPESVIRUS 4 (EPSTEIN-BARR VIRUS)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31486.00

構造登録者

Tarbouriech, N.,Buisson, M.,Seigneurin, J.-M.,Cusack, S.,Burmeister, W.P. (登録日: 2005-05-24, 公開日: 2005-09-15, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.7 Å)