The Crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms

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

Research output: Contribution to journalArticlepeer-review

Abstract

The crystal structure of C. elegans Ap4A hydrolase has been determined for the free enzyme and a binary complex at 2.0 Å and 1.8 Å, respectively. Ap4A hydrolase has a key role in regulating the intracellular Ap4A levels and hence potentially the cellular response to metabolic stress and/or differentiation and apoptosis via the Ap3A/Ap4A ratio. The structures reveal that the enzyme has the mixed α/β fold of the Nudix family and also show how the enzyme binds and locates its substrate with respect to the catalytic machinery of the Nudix motif. These results suggest how the enzyme can catalyze the hydrolysis of a range of related dinucleoside tetraphosphate, but not triphosphate, compounds through precise orientation of key elements of the substrate.

Original languageEnglish (US)
Pages (from-to)589-600
Number of pages12
JournalStructure
Volume10
Issue number4
DOIs
StatePublished - 2002
Externally publishedYes

Keywords

  • ApA hydrolase
  • Asymmetric cleavage
  • Caenorhabditis elegans
  • Magnesium cluster
  • Nudix family
  • Substrate pocket

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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