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Publication Abstract from PubMed

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 Mg(2+), 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.

Structure of a coenzyme A pyrophosphatase from Deinococcus radiodurans: a member of the Nudix family.,Kang LW, Gabelli SB, Bianchet MA, Xu WL, Bessman MJ, Amzel LM J Bacteriol. 2003 Jul;185(14):4110-8. PMID:12837785^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.