1N2A

Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site

Summary for 1N2A

• Entry DOI: 10.2210/pdb1n2a/pdb
• Descriptor: Glutathione S-transferase, GLUTATHIONE SULFONIC ACID (3 entities in total)
• Functional Keywords: transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A9D2
• Total number of polymer chains: 2
• Total formula weight: 46503.33

Authors

Rife, C.L.,Parsons, J.F.,Xiao, G.,Gilliland, G.L.,Armstrong, R.N. (deposition date: 2002-10-22, release date: 2003-11-04, Last modification date: 2024-02-14)

Primary citation

Rife, C.L.,Parsons, J.F.,Xiao, G.,Gilliland, G.L.,Armstrong, R.N.
Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli
Proteins, 53:777-782, 2003

PubMed 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 enzyme consists of two domains. The N-terminal region (domain I) has a thioredoxin-like alpha/beta-fold, while the C-terminal domain (domain II) is all alpha-helical. The majority of the consensus residues (12/17) reside in the N-terminal domain. Fifteen of the 17 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 alpha/beta domain and the C-terminal domain. The conservation of two key residues for the recognition motif for the gamma-glutamyl-portion of GSH indicates that the homologues may interact with GSH or GSH analogues such as glutathionylspermidine or alpha-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 glutathionylspermidine and selenium biochemistry, respectively.

PubMed: 14635120
DOI: 10.1002/prot.10452

Experimental method

X-RAY DIFFRACTION (1.9 Å)