Document Type
Article
Publication Date
8-1-2000
Publication Title
Acta Crystallographica Section D: Biological Crystallography
Abstract
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 molecular replacement and Patterson methods. In general, structures containing multiple copies of molecules in the asymmetric unit are difficult to determine. In this case, the two trimers in the asymmetric unit are parallel to each other and use of the Patterson function greatly simplified the structure solution.
Repository Citation
Vitali, Jacqueline; Vorobyova, Tatyana; Websterb, Gordon; and Kantrowitza, Evan R., "Crystallization and Structure Determination of the Catalytic Trimer of Methanococcus Jannaschii Aspartate Transcarbamoylase" (2000). Physics Faculty Publications. 185.
https://engagedscholarship.csuohio.edu/sciphysics_facpub/185
Original Citation
Vitali, J., Vorobyova, T., Webster, G. and Kantrowitz, E.R. (2000) Crystallization and Structure Determination of the Catalytic Trimer of Methanococcus Jannaschii Aspartate Transcarbamoylase. Acta Crystallographica D56, 1061-1063.
DOI
10.1107/S0907444900008167
Version
Publisher's PDF
Publisher's Statement
©2000 International Union of Crystallography
Volume
D56
Issue
8
Comments
This work was supported in part by the National Institutes of Health Grant GM26237.