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Literature summary for 2.5.1.54 extracted from

  • Light, S.H.; Halavaty, A.S.; Minasov, G.; Shuvalova, L.; Anderson, W.F.
    Structural analysis of a 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase with an N-terminal chorismate mutase-like regulatory domain (2012), Protein Sci., 21, 887-895.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Listeria monocytogenes

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Metals/Ions Comment Organism Structure
Mn2+ a manganese ion is present at the active site, crystallization data Listeria monocytogenes

Organism

Organism UniProt Comment Textmining
Listeria monocytogenes
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