1NQZ

The structure of a CoA pyrophosphatase from D. Radiodurans complexed with a magnesium ion

1NQZ の概要

• エントリーDOI: 10.2210/pdb1nqz/pdb
• 関連するPDBエントリー: 1NQY
• 分子名称: CoA pyrophosphatase (MutT/nudix family protein), MAGNESIUM ION (3 entities in total)
• 機能のキーワード: nudix, mutt, pyrophosphatase, coa, d.radiodurans, hydrolase
• 由来する生物種: Deinococcus radiodurans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21297.53

構造登録者

Kang, L.W.,Gabelli, S.B.,Bianchet, M.A.,Xu, W.L.,Bessman, M.J.,Amzel, L.M. (登録日: 2003-01-23, 公開日: 2003-05-13, 最終更新日: 2023-08-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)