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Crystallization And Structure Determination Of The Catalytic Trimer Of Methanococcus Jannaschii Aspartate Transcarbamoylase, Jacqueline Vitali, Tatyana Vorobyova, Gordon Websterb, Evan R. Kantrowitza

Physics Faculty Publications

Aspartate transcarbamoylase (ATCase) catalyzes the first step in the pyrimidine biosynthetic pathway, the reaction between carbamoyl phosphate and L-aspartate to form N-carbamoyl-L-aspartate and phosphate. The structural analysis of the ATCase catalytic trimer from Methanococcus jannaschii, a unicellular thermophilic archaeabacterium, has been undertaken in order to gain insight into the structural features that are responsible for the thermostability of the enzyme. As a first step, the catalytic trimer was crystallized in space group R32, with unit-cell parameters a = b = 265.3, c = 195.5 Å and two trimers in the asymmetric unit. Its structure was determined using …