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The structure of a CoA pyrophosphatase from D. Radiodurans complexed with a magnesium ionThe structure of a CoA pyrophosphatase from D. Radiodurans complexed with a magnesium ion
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGene 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. References |
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