1NQY

The structure of a CoA pyrophosphatase from D. Radiodurans

Summary for 1NQY

• Entry DOI: 10.2210/pdb1nqy/pdb
• Related: 1NQZ
• Descriptor: CoA pyrophosphatase (MutT/nudix family protein) (2 entities in total)
• Functional Keywords: nudix, pyrophosphatase, dr1184, coa, hydrolase
• Biological source: Deinococcus radiodurans
• Total number of polymer chains: 1
• Total formula weight: 21273.23

Authors

Kang, L.W.,Gabelli, S.B.,Bianchet, M.A.,Xu, W.L.,Bessman, M.J.,Amzel, L.M. (deposition date: 2003-01-23, release date: 2003-05-13, Last modification date: 2024-02-14)

Primary citation

Kang, L.W.,Gabelli, S.B.,Bianchet, M.A.,Xu, W.L.,Bessman, M.J.,Amzel, L.M.
Structure of a coenzyme A pyrophosphatase from Deinococcus radiodurans: a member of the Nudix family.
J.Bacteriol., 185:4110-4118, 2003

PubMed 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 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.

PubMed: 12837785
DOI: 10.1128/JB.185.14.4110-4118.2003

Experimental method

X-RAY DIFFRACTION (2.09 Å)