Structure of a coenzyme A pyrophosphatase from Deinococcus radiodurans: A member of the Nudix family

Lin Woo Kang, Sandra B. Gabelli, Mario A. Bianchet, Wen Lian Xu, Maurice J. Bessman, L. Mario Amzel

Research output: Contribution to journalArticlepeer-review

Abstract

Gene Dr1184 from Deinococcus radiodurans codes for a Nudix enzyme (DR-CoAse) that hydrolyzes the pyrophosphate moiety of coenzyme A (CoA). Nudix enzymes with the same specificity have been found in yeast, humans, and mice. The three-dimensional structure of DR-CoAse, the first of a Nudix hydrolase with this specificity, reveals that this enzyme contains, in addition to the fold observed in other Nudix enzymes, insertions that are characteristic of a CoA-hydrolyzing Nudix subfamily. The structure of the complex of the enzyme with Mg2+, its activating cation, reveals the position of the catalytic site. A helix, part of the N-terminal insertion, partially occludes the binding site and has to change its position to permit substrate binding. Comparison of the structure of DR-CoAse to those of other Nudix enzymes, together with the location in the structure of the sequence characteristic of CoAses, suggests a mode of binding of the substrate to the enzyme that is compatible with all available data.

Original languageEnglish (US)
Pages (from-to)4110-4118
Number of pages9
JournalJournal of bacteriology
Volume185
Issue number14
DOIs
StatePublished - Jul 2003

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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