Work

Crystallization and structure determination of the catalytic trimer ofMethanococcus jannaschiiaspartate transcarbamoylase

Year: 2000

Type: article

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 A 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.

Source: Acta Crystallographica Section D Biological Crystallography

DOI: 10.1107/s0907444900008167

Authors: Jacqueline Vitali, Tatyana Vorobyova, Gordon Webster, Evan R. Kantrowitz

Institutions: Boston College, Beth Israel Deaconess Medical Center, Harvard University

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Awards: G2333914548, The Molecular Basis of Cellular Control Mechanisms