TY - JOUR
T1 - Structure of a coenzyme A pyrophosphatase from Deinococcus radiodurans
T2 - A member of the Nudix family
AU - Kang, Lin Woo
AU - Gabelli, Sandra B.
AU - Bianchet, Mario A.
AU - Xu, Wen Lian
AU - Bessman, Maurice J.
AU - Amzel, L. Mario
PY - 2003/7
Y1 - 2003/7
N2 - 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.
AB - 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.
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U2 - 10.1128/JB.185.14.4110-4118.2003
DO - 10.1128/JB.185.14.4110-4118.2003
M3 - Article
C2 - 12837785
AN - SCOPUS:0037816373
SN - 0021-9193
VL - 185
SP - 4110
EP - 4118
JO - Journal of bacteriology
JF - Journal of bacteriology
IS - 14
ER -