The molecule diadenosine tetraphosphate (Ap4A) has been suggested to be a component of the cellular response to metabolic stress and/or, via the intracellular Ap3A/Ap4A ratio, to be involved in differentiation and apoptosis. Thus, the enzyme Ap4A hydrolase has a key metabolic role through regulation of the intracellular Ap4A levels. Crystals of this enzyme from the nematode Caenorhabditis elegans have been obtained in the presence of a non-hydrolysable substrate analogue, AppCH2ppA. The crystals belong to space group P21, unit-cell parameters a = 57.6, b = 36.8, c = 68.9 Å, β = 114.2°, and diffract to approximately 2.0 Å. Determination of the structure of this complex will provide insights into the substrate specificity and catalytic activity of this class of enzymes.
|Original language||English (US)|
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|State||Published - 2002|
ASJC Scopus subject areas
- Structural Biology