1nqz
The structure of a CoA pyrophosphatase from D. Radiodurans complexed with a magnesium ion
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| , resolution 1.7Å | |||||||
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| Ligands: | |||||||
| Gene: | dr1184 (Deinococcus radiodurans) | ||||||
| Activity: | Nucleotide diphosphatase, with EC number 3.6.1.9 | ||||||
| Related: | 1NQY
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1NQZ is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.
ReferenceReference
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
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