PDBsum entry 1a0f

Transferase

PDB id: 1a0f

Contents

Protein chains

201 a.a. *

Ligands

GTS ×2

Waters ×174

* Residue conservation analysis

PDB id:

1a0f

Name:

Transferase

Title:

Crystal structure of glutathione s-transferase from escherichia coli complexed with glutathionesulfonic acid

Structure:

Glutathione s-transferase. Chain: a, b. Fragment: glutathione-binding domain. Synonym: gst, glutathione transferase. Engineered: yes

Source:

Escherichia coli k12. Organism_taxid: 83333. Strain: k-12. Gene: gst. Expressed in: escherichia coli k12. Expression_system_taxid: 83333.

Biol. unit:

Dimer (from PDB file)

Resolution:

2.10Å R-factor: 0.183 R-free: 0.245

Authors:

M.Nishida,S.Harada,S.Noguchi,H.Inoue,K.Takahashi,Y.Satow

Key ref:

M.Nishida et al. (1998). Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106. J Mol Biol, 281, 135-147. PubMed id: 9680481 DOI: 10.1006/jmbi.1998.1927

Date:

29-Nov-97 Release date: 13-Jan-99

Protein chains

P0A9D2  (GSTA_ECOLI) -  Glutathione S-transferase GstA from Escherichia coli (strain K12)

Seq: 201 a.a.

Struc: 201 a.a.

Enzyme reactions

• Enzyme class: E.C.2.5.1.18 - glutathione transferase.
• Reaction: RX + glutathione = an S-substituted glutathione + a halide anion + H⁺

RX (Bound ligand (Het Group name = GTS) matches with 86.96% similarity) + glutathione = S-substituted glutathione + halide anion + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1006/jmbi.1998.1927

J Mol Biol 281:135-147 (1998)

PubMed id: 9680481

Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106.

M.Nishida, S.Harada, S.Noguchi, Y.Satow, H.Inoue, K.Takahashi.

ABSTRACT

Cytosolic glutathione S-transferase is a family of multi-functional enzymes involved in the detoxification of a large variety of xenobiotic and endobiotic compounds through glutathione conjugation. The three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate, N-(N-L-gamma-glutamyl-3-sulfo-L-alanyl)-glycine, has been determined by the multiple isomorphous replacement method and refined to a crystallographic R factor of 0.183 at 2.1 A resolution.The E. coli enzyme is a globular homodimer with dimensions of 58 Ax56 Ax52 A. Each subunit, consisting of a polypeptide of 201 amino acid residues, is divided into a smaller N-terminal domain (residues 1 to 80) and a larger C-terminal one (residues 89 to 201). The core of the N-terminal domain is constructed by a four-stranded beta-sheet and two alpha-helices, and that of the C-terminal one is constructed by a right-handed bundle of four alpha-helices. Glutathione sulfonate, a competitive inhibitor against glutathione, is bound in a cleft between the N and C-terminal domains. Therefore, the E. coli enzyme conserves overall constructions common to the eukaryotic enzymes, in its polypeptide fold, dimeric assembly, and glutathione-binding site. In the case of the eukaryotic enzymes, tyrosine and serine residues near the N terminus are located in the proximity of the sulfur atom of the bound glutathione, and are proposed to be catalytically essential. In the E. coli enzyme, Tyr5 and Ser11 corresponding to these residues are not involved in the interaction with the inhibitor, although they are located in the vicinity of catalytic site. Instead, Cys10 N and His106 Nepsilon2 atoms are hydrogen-bonded to the sulfonate group of the inhibitor. On the basis of this structural study, Cys10 and His106 are ascribed to the catalytic residues that are distinctive from the family of the eukaryotic enzymes. We propose that glutathione S-transferases have diverged from a common origin and acquired different catalytic apparatuses in the process of evolution.

Selected figure(s)

Figure 5.
Figure 5. Schematic drawing for interactions between E. coli GST and glutathione sulfonate. Water molecules located in the GSH-bind- ing site are shown as Wat. Hydro- gen bonds are drawn as broken lines, and their distances are given in Å . Residues from the accompa- nying subunit are indicated by asterisks.

Figure 7.
Figure 7. Stereo views of the cata- lytic site of E. coli GST superposed on the structures of eukaryotic theta and alpha GSTs. The ligand molecules, glutathione sulfonate in E. coli GST, S-hexyl-glutathione in theta GST from A. thaliana (Reinemer et al., 1996), and S-ben- zyl-glutathione in human GST alpha 1-1 (Sinning et al., 1993), and the C a atoms of the enzymes are superposed in the Figure. The structure for the liganded E. coli GST is colored red, and those for the theta (a) and alpha (b) GSTs are in green and blue, respectively. Residues from the accompanying subunit are shown by asterisks. The ligand molecules are in light colors. Hydrogen bonds formed in the catalytic site of E. coli and alpha are drawn as dotted lines.

The above figures are reprinted by permission from Elsevier: J Mol Biol (1998, 281, 135-147) copyright 1998.

Figures were selected by an automated process.