Cloned (Comment) | Organism |
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expression in Escherichia coli | Listeria monocytogenes |
Crystallization (Comment) | Organism |
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structures in complex with Mn2+ and Mn+ and phosphoenolpyruvate, to 1.95 A resolution. The domains assemble as a tetramer, from either side of which chorismate mutase-like regulatory domains asymmetrically emerge to form a pair of dimers. Domain organization suggests that chorismate/prephenate binding promotes a stable interaction between the discrete regulatory and catalytic domains and supports a mechanism of allosteric inhibition similar to tyrosine/phenylalanine control of a related DAHPS class. The catalytic domain adopts a classic TIM barrel (alpha/beta)8 fold. The active site is located on the inside of the C-terminal end of the barrel and is formed by several alpha-beta-connecting loops and two beta-strands. In the holo structure, a manganese ion is present at the active site. In the phosphoenolpyruvate structure, the substrate is adjacent to the manganese ion in a similar position as has been observed in related enzymes | Listeria monocytogenes |
Metals/Ions | Comment | Organism | Structure |
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Mn2+ | a manganese ion is present at the active site, crystallization data | Listeria monocytogenes |
Organism | UniProt | Comment | Textmining |
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Listeria monocytogenes | - |
- |
- |