Cloned (Comment) | Organism |
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- |
Saccharomyces cerevisiae |
Crystallization (Comment) | Organism |
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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 | 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 79.5) | 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 | 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 | UniProt | Comment | Textmining |
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Saccharomyces cerevisiae | P53550 | - |
- |