Crystallization of a complex of Caenorhabditis elegans diadenosine tetraphosphate hydrolase and a non-hydrolysable substrate analogue, AppCH2ppA

Scott Bailey, Svetlana E. Sedelnikova, G. Michael Blackburn, Hend M. Abdelghany, Alexander G. McLennan, John B. Rafferty

Research output: Contribution to journalArticlepeer-review

Abstract

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 languageEnglish (US)
Pages (from-to)526-528
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume58
Issue number3
DOIs
StatePublished - 2002
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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