1n2a

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

Structural highlights

1n2a is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GSTA_ECOLI Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity.[1] [2] [3] [4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Nishida M, Kong KH, Inoue H, Takahashi K. Molecular cloning and site-directed mutagenesis of glutathione S-transferase from Escherichia coli. The conserved tyrosyl residue near the N terminus is not essential for catalysis. J Biol Chem. 1994 Dec 23;269(51):32536-41. PMID:7798255
  2. ↑ Arca P, Garcia P, Hardisson C, Suarez JE. Purification and study of a bacterial glutathione S-transferase. FEBS Lett. 1990 Apr 9;263(1):77-9. PMID:2185038
  3. ↑ Kanai T, Takahashi K, Inoue H. Three distinct-type glutathione S-transferases from Escherichia coli important for defense against oxidative stress. J Biochem. 2006 Nov;140(5):703-11. Epub 2006 Oct 3. PMID:17018556 doi:http://dx.doi.org/10.1093/jb/mvj199
  4. ↑ Wang XY, Zhang ZR, Perrett S. Characterization of the activity and folding of the glutathione transferase from Escherichia coli and the roles of residues Cys(10) and His(106). Biochem J. 2009 Jan 1;417(1):55-64. doi: 10.1042/BJ20071702. PMID:18778244 doi:http://dx.doi.org/10.1042/BJ20071702

1n2a, resolution 1.90Å

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OCA
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