Conserved Structural Elements in Glutathione Transferase Homologues Encoded in the Genome of Escherichia Coli

Published

December 1, 2003

Author(s)

C L. Rife, J F. Parsons, G Xiao, G L. Gilliland, R N. Armstrong

Abstract

Multiple sequence alignments of the eight glutathione (GSH) transferase homologues encoded in the genome of Escherichia coli were used to define a consensus sequence for the proteins. The consensus sequence was analyzed in the context of the three-dimensional structure of the gst gene product (EGST) obtained from two different crystal forms of the enzyme. The majority of the consensus residues (12/17) reside in the N-terminal domain. Fifteen of the seventeen residues are involved in hydrophobic core interactions, turns, or electrostatic interactions between the two domains. The results suggest that all of the homologues retain a well-defined group of structural elements both in and between the N-terminal a/b domain and the all-helical C-terminal domain. The conservation of two key residues for the recognition motif for the g-glutamyl-portion of GSH indicates that the homologues may interact with GSH or GSH analogues such as glutathionylspermidine or a-amino acids. The genome context of two of the homologues forms the basis for a hypothesis that the B2989 and yibF gene products are involved in glutathionlyspermidine and selenium biochemistry, respectively.

Citation

Proteins-Structure Function And Genetics

Volume

53

Issue

4

Pub Type

Journals

Keywords

crystal structure, Escherichia coli, glutathione, glutathione S-transferase, glutathione-binding, sequence analysis

Citation

Rife, C. , Parsons, J. , Xiao, G. , Gilliland, G. and Armstrong, R. (2003), Conserved Structural Elements in Glutathione Transferase Homologues Encoded in the Genome of Escherichia Coli, Proteins-Structure Function And Genetics (Accessed April 23, 2024)