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.

Comments

This work was supported in part by the National Institutes of Health Grant GM26237.

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

Volume

D56

Issue

8

Share

COinS