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Literature summary for 3.6.1.62 extracted from

  • Aglietti, R.A.; Floor, S.N.; McClendon, C.L.; Jacobson, M.P.; Gross, J.D.
    Active site conformational dynamics are coupled to catalysis in the mRNA decapping enzyme Dcp2 (2013), Structure, 21, 1571-1580.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of wild-type, and E198Q and E153Q catalytic glutamate mutants of the Dcp2 Nudix domain, to 2.1A, 1.8 A and 1.7 A resolution, respectively. Conserved glutamate residues E152, E153, and E198 coordinate a magnesium ion through a water mediated contact, while E149 directly contacts the metal. A conserved metal binding loop on the catalytic domain undergoes conformational changes during the catalytic cycle Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E153Q mutant has 3 molecules in the asymmetric unit. There is clear electron density for an octahedrally coordinated Mg2+ in the structure, similar to wild-type. Mutant is severely catalytically compromised and displays a linear dependence on pH over the range studied (pH 7–9.5) Saccharomyces cerevisiae
E198Q mutant lacks clear density for a metal ion in the active site and fails to crystallize in the presence of any divalent cation Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ conserved glutamate residues E152, E153, and E198 coordinate a magnesium ion through a water mediated contact, while E149 directly contacts the metal Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P53550
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