Structural and functional characterisation of the methionine adenosyltransferase from Thermococcus kodakarensis.

ABSTRACT:

Background

Methionine adenosyltransferases catalyse the synthesis of S-adenosylmethionine, a cofactor abundant in all domains of life. In contrast to the enzymes from bacteria and eukarya that show high sequence similarity, methionine adenosyltransferases from archaea diverge on the amino acid sequence level and only few conserved residues are retained.

Results

We describe the initial characterisation and the crystal structure of the methionine adenosyltransferase from the hyperthermophilic archaeon Thermococcus kodakarensis. As described for other archaeal methionine adenosyltransferases the enzyme is a dimer in solution and shows high temperature stability. The overall structure is very similar to that of the bacterial and eukaryotic enzymes described, with some additional

SUBMITTER: Schlesier J 

PROVIDER: S-EPMC3853416 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature